A 31-kDa seminal plasma heparin–binding protein reduces cold shock stress during cryopreservation of cross-bred cattle bull semen
In the present study, a 31-kDa protein, purified from cattle bull seminal plasma heparin–binding proteins (SP-HBP), was characterized by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and mass spectrometry. Raw semen of six cross-bred bulls was treated with 31-kDa HBP before cryopreservat...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Patel, M.K. [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2016transfer abstract |
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| Schlagwörter: |
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| Umfang: |
8 |
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| Übergeordnetes Werk: |
Enthalten in: Multi-source monitoring information fusion method for dam health diagnosis based on Wasserstein distance - Chen, Anyi ELSEVIER, 2023, an international journal of animal reproduction, Amsterdam [u.a.] |
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| Übergeordnetes Werk: |
volume:86 ; year:2016 ; number:6 ; day:1 ; month:10 ; pages:1599-1606 ; extent:8 |
| Links: |
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| DOI / URN: |
10.1016/j.theriogenology.2016.05.020 |
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ELV029433614 |
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| 245 | 1 | 0 | |a A 31-kDa seminal plasma heparin–binding protein reduces cold shock stress during cryopreservation of cross-bred cattle bull semen |
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| 520 | |a In the present study, a 31-kDa protein, purified from cattle bull seminal plasma heparin–binding proteins (SP-HBP), was characterized by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and mass spectrometry. Raw semen of six cross-bred bulls was treated with 31-kDa HBP before cryopreservation to observe its effect on motility, viability, hypo-osmotic swelling test, acrosome integrity, in vitro capacitation/acrosome reaction, and oxidative stress at pre-freeze and frozen–thawed phases of cryopreservation. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis of 31-kDa protein eluted and purified from SP-HBP (separated on acrylamide gels) resulted in a single band of 40 kDa. In matrix-assisted laser desorption/ionization–time of flight analysis, 12 peptides were identified with matching significantly (P < 0.05) to interlukin-6 of bovine with a top score of 55. Addition of 25 μg/mL of fluorescein isothiocyanate–conjugated 31-kDa protein to raw semen and incubation at 37 °C for 20 minutes before cryopreservation resulted in its binding mainly to head region. Treatment of semen with 31-kDa HBP resulted in a significant (P < 0.05) average increase of 9.2%, 6.8%, and 11.7% and 5.5%, 6.5%, and 11.0% in motile, viable, hypo-osmotic swelling–responsive spermatozoa in six bulls at pre-freeze and frozen–thawed phases of cryopreservation, respectively. Percentage of spermatozoa with intact acrosomes nonsignificantly enhanced in the semen treated with 31-kDa HBP at both phases of cryopreservation. An average nonsignificant increase of 3.1% in in vitro capacitated and acrosome-reacted spermatozoa was obtained in semen supplemented with 31-kDa HBP. Addition of 31-kDa HBP also nonsignificantly reduced Malonadialdehyde (MDA) level by 10.7 and 19.3 μM/109 spermatozoa in prefrozen and frozen–thawed semen, respectively. The results obtained here indicate to conclude that treatment of cross-bred cattle bull semen with 31-kDa HBP protects the spermatozoa from cold shock effect by coating the sperm surface. | ||
| 520 | |a In the present study, a 31-kDa protein, purified from cattle bull seminal plasma heparin–binding proteins (SP-HBP), was characterized by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and mass spectrometry. Raw semen of six cross-bred bulls was treated with 31-kDa HBP before cryopreservation to observe its effect on motility, viability, hypo-osmotic swelling test, acrosome integrity, in vitro capacitation/acrosome reaction, and oxidative stress at pre-freeze and frozen–thawed phases of cryopreservation. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis of 31-kDa protein eluted and purified from SP-HBP (separated on acrylamide gels) resulted in a single band of 40 kDa. In matrix-assisted laser desorption/ionization–time of flight analysis, 12 peptides were identified with matching significantly (P < 0.05) to interlukin-6 of bovine with a top score of 55. Addition of 25 μg/mL of fluorescein isothiocyanate–conjugated 31-kDa protein to raw semen and incubation at 37 °C for 20 minutes before cryopreservation resulted in its binding mainly to head region. Treatment of semen with 31-kDa HBP resulted in a significant (P < 0.05) average increase of 9.2%, 6.8%, and 11.7% and 5.5%, 6.5%, and 11.0% in motile, viable, hypo-osmotic swelling–responsive spermatozoa in six bulls at pre-freeze and frozen–thawed phases of cryopreservation, respectively. Percentage of spermatozoa with intact acrosomes nonsignificantly enhanced in the semen treated with 31-kDa HBP at both phases of cryopreservation. An average nonsignificant increase of 3.1% in in vitro capacitated and acrosome-reacted spermatozoa was obtained in semen supplemented with 31-kDa HBP. Addition of 31-kDa HBP also nonsignificantly reduced Malonadialdehyde (MDA) level by 10.7 and 19.3 μM/109 spermatozoa in prefrozen and frozen–thawed semen, respectively. The results obtained here indicate to conclude that treatment of cross-bred cattle bull semen with 31-kDa HBP protects the spermatozoa from cold shock effect by coating the sperm surface. | ||
| 650 | 7 | |a semen |2 Elsevier | |
| 650 | 7 | |a 31 kDa |2 Elsevier | |
| 650 | 7 | |a cattle bull |2 Elsevier | |
| 650 | 7 | |a SP-HBP |2 Elsevier | |
| 650 | 7 | |a cold shock stress |2 Elsevier | |
| 700 | 1 | |a Cheema, R.S. |4 oth | |
| 700 | 1 | |a Bansal, A.K. |4 oth | |
| 700 | 1 | |a Gandotra, V.K. |4 oth | |
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10.1016/j.theriogenology.2016.05.020 doi GBVA2016002000002.pica (DE-627)ELV029433614 (ELSEVIER)S0093-691X(16)30220-5 DE-627 ger DE-627 rakwb eng 590 590 DE-600 070 004 VZ LING DE-30 fid 54.00 bkl 53.71 bkl Patel, M.K. verfasserin aut A 31-kDa seminal plasma heparin–binding protein reduces cold shock stress during cryopreservation of cross-bred cattle bull semen 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In the present study, a 31-kDa protein, purified from cattle bull seminal plasma heparin–binding proteins (SP-HBP), was characterized by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and mass spectrometry. Raw semen of six cross-bred bulls was treated with 31-kDa HBP before cryopreservation to observe its effect on motility, viability, hypo-osmotic swelling test, acrosome integrity, in vitro capacitation/acrosome reaction, and oxidative stress at pre-freeze and frozen–thawed phases of cryopreservation. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis of 31-kDa protein eluted and purified from SP-HBP (separated on acrylamide gels) resulted in a single band of 40 kDa. In matrix-assisted laser desorption/ionization–time of flight analysis, 12 peptides were identified with matching significantly (P < 0.05) to interlukin-6 of bovine with a top score of 55. Addition of 25 μg/mL of fluorescein isothiocyanate–conjugated 31-kDa protein to raw semen and incubation at 37 °C for 20 minutes before cryopreservation resulted in its binding mainly to head region. Treatment of semen with 31-kDa HBP resulted in a significant (P < 0.05) average increase of 9.2%, 6.8%, and 11.7% and 5.5%, 6.5%, and 11.0% in motile, viable, hypo-osmotic swelling–responsive spermatozoa in six bulls at pre-freeze and frozen–thawed phases of cryopreservation, respectively. Percentage of spermatozoa with intact acrosomes nonsignificantly enhanced in the semen treated with 31-kDa HBP at both phases of cryopreservation. An average nonsignificant increase of 3.1% in in vitro capacitated and acrosome-reacted spermatozoa was obtained in semen supplemented with 31-kDa HBP. Addition of 31-kDa HBP also nonsignificantly reduced Malonadialdehyde (MDA) level by 10.7 and 19.3 μM/109 spermatozoa in prefrozen and frozen–thawed semen, respectively. The results obtained here indicate to conclude that treatment of cross-bred cattle bull semen with 31-kDa HBP protects the spermatozoa from cold shock effect by coating the sperm surface. In the present study, a 31-kDa protein, purified from cattle bull seminal plasma heparin–binding proteins (SP-HBP), was characterized by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and mass spectrometry. Raw semen of six cross-bred bulls was treated with 31-kDa HBP before cryopreservation to observe its effect on motility, viability, hypo-osmotic swelling test, acrosome integrity, in vitro capacitation/acrosome reaction, and oxidative stress at pre-freeze and frozen–thawed phases of cryopreservation. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis of 31-kDa protein eluted and purified from SP-HBP (separated on acrylamide gels) resulted in a single band of 40 kDa. In matrix-assisted laser desorption/ionization–time of flight analysis, 12 peptides were identified with matching significantly (P < 0.05) to interlukin-6 of bovine with a top score of 55. Addition of 25 μg/mL of fluorescein isothiocyanate–conjugated 31-kDa protein to raw semen and incubation at 37 °C for 20 minutes before cryopreservation resulted in its binding mainly to head region. Treatment of semen with 31-kDa HBP resulted in a significant (P < 0.05) average increase of 9.2%, 6.8%, and 11.7% and 5.5%, 6.5%, and 11.0% in motile, viable, hypo-osmotic swelling–responsive spermatozoa in six bulls at pre-freeze and frozen–thawed phases of cryopreservation, respectively. Percentage of spermatozoa with intact acrosomes nonsignificantly enhanced in the semen treated with 31-kDa HBP at both phases of cryopreservation. An average nonsignificant increase of 3.1% in in vitro capacitated and acrosome-reacted spermatozoa was obtained in semen supplemented with 31-kDa HBP. Addition of 31-kDa HBP also nonsignificantly reduced Malonadialdehyde (MDA) level by 10.7 and 19.3 μM/109 spermatozoa in prefrozen and frozen–thawed semen, respectively. The results obtained here indicate to conclude that treatment of cross-bred cattle bull semen with 31-kDa HBP protects the spermatozoa from cold shock effect by coating the sperm surface. semen Elsevier 31 kDa Elsevier cattle bull Elsevier SP-HBP Elsevier cold shock stress Elsevier Cheema, R.S. oth Bansal, A.K. oth Gandotra, V.K. oth Enthalten in Elsevier Science Chen, Anyi ELSEVIER Multi-source monitoring information fusion method for dam health diagnosis based on Wasserstein distance 2023 an international journal of animal reproduction Amsterdam [u.a.] (DE-627)ELV009476539 volume:86 year:2016 number:6 day:1 month:10 pages:1599-1606 extent:8 https://doi.org/10.1016/j.theriogenology.2016.05.020 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-LING SSG-OPC-BBI 54.00 Informatik: Allgemeines VZ 53.71 Theoretische Nachrichtentechnik VZ AR 86 2016 6 1 1001 1599-1606 8 045F 590 |
| spelling |
10.1016/j.theriogenology.2016.05.020 doi GBVA2016002000002.pica (DE-627)ELV029433614 (ELSEVIER)S0093-691X(16)30220-5 DE-627 ger DE-627 rakwb eng 590 590 DE-600 070 004 VZ LING DE-30 fid 54.00 bkl 53.71 bkl Patel, M.K. verfasserin aut A 31-kDa seminal plasma heparin–binding protein reduces cold shock stress during cryopreservation of cross-bred cattle bull semen 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In the present study, a 31-kDa protein, purified from cattle bull seminal plasma heparin–binding proteins (SP-HBP), was characterized by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and mass spectrometry. Raw semen of six cross-bred bulls was treated with 31-kDa HBP before cryopreservation to observe its effect on motility, viability, hypo-osmotic swelling test, acrosome integrity, in vitro capacitation/acrosome reaction, and oxidative stress at pre-freeze and frozen–thawed phases of cryopreservation. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis of 31-kDa protein eluted and purified from SP-HBP (separated on acrylamide gels) resulted in a single band of 40 kDa. In matrix-assisted laser desorption/ionization–time of flight analysis, 12 peptides were identified with matching significantly (P < 0.05) to interlukin-6 of bovine with a top score of 55. Addition of 25 μg/mL of fluorescein isothiocyanate–conjugated 31-kDa protein to raw semen and incubation at 37 °C for 20 minutes before cryopreservation resulted in its binding mainly to head region. Treatment of semen with 31-kDa HBP resulted in a significant (P < 0.05) average increase of 9.2%, 6.8%, and 11.7% and 5.5%, 6.5%, and 11.0% in motile, viable, hypo-osmotic swelling–responsive spermatozoa in six bulls at pre-freeze and frozen–thawed phases of cryopreservation, respectively. Percentage of spermatozoa with intact acrosomes nonsignificantly enhanced in the semen treated with 31-kDa HBP at both phases of cryopreservation. An average nonsignificant increase of 3.1% in in vitro capacitated and acrosome-reacted spermatozoa was obtained in semen supplemented with 31-kDa HBP. Addition of 31-kDa HBP also nonsignificantly reduced Malonadialdehyde (MDA) level by 10.7 and 19.3 μM/109 spermatozoa in prefrozen and frozen–thawed semen, respectively. The results obtained here indicate to conclude that treatment of cross-bred cattle bull semen with 31-kDa HBP protects the spermatozoa from cold shock effect by coating the sperm surface. In the present study, a 31-kDa protein, purified from cattle bull seminal plasma heparin–binding proteins (SP-HBP), was characterized by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and mass spectrometry. Raw semen of six cross-bred bulls was treated with 31-kDa HBP before cryopreservation to observe its effect on motility, viability, hypo-osmotic swelling test, acrosome integrity, in vitro capacitation/acrosome reaction, and oxidative stress at pre-freeze and frozen–thawed phases of cryopreservation. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis of 31-kDa protein eluted and purified from SP-HBP (separated on acrylamide gels) resulted in a single band of 40 kDa. In matrix-assisted laser desorption/ionization–time of flight analysis, 12 peptides were identified with matching significantly (P < 0.05) to interlukin-6 of bovine with a top score of 55. Addition of 25 μg/mL of fluorescein isothiocyanate–conjugated 31-kDa protein to raw semen and incubation at 37 °C for 20 minutes before cryopreservation resulted in its binding mainly to head region. Treatment of semen with 31-kDa HBP resulted in a significant (P < 0.05) average increase of 9.2%, 6.8%, and 11.7% and 5.5%, 6.5%, and 11.0% in motile, viable, hypo-osmotic swelling–responsive spermatozoa in six bulls at pre-freeze and frozen–thawed phases of cryopreservation, respectively. Percentage of spermatozoa with intact acrosomes nonsignificantly enhanced in the semen treated with 31-kDa HBP at both phases of cryopreservation. An average nonsignificant increase of 3.1% in in vitro capacitated and acrosome-reacted spermatozoa was obtained in semen supplemented with 31-kDa HBP. Addition of 31-kDa HBP also nonsignificantly reduced Malonadialdehyde (MDA) level by 10.7 and 19.3 μM/109 spermatozoa in prefrozen and frozen–thawed semen, respectively. The results obtained here indicate to conclude that treatment of cross-bred cattle bull semen with 31-kDa HBP protects the spermatozoa from cold shock effect by coating the sperm surface. semen Elsevier 31 kDa Elsevier cattle bull Elsevier SP-HBP Elsevier cold shock stress Elsevier Cheema, R.S. oth Bansal, A.K. oth Gandotra, V.K. oth Enthalten in Elsevier Science Chen, Anyi ELSEVIER Multi-source monitoring information fusion method for dam health diagnosis based on Wasserstein distance 2023 an international journal of animal reproduction Amsterdam [u.a.] (DE-627)ELV009476539 volume:86 year:2016 number:6 day:1 month:10 pages:1599-1606 extent:8 https://doi.org/10.1016/j.theriogenology.2016.05.020 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-LING SSG-OPC-BBI 54.00 Informatik: Allgemeines VZ 53.71 Theoretische Nachrichtentechnik VZ AR 86 2016 6 1 1001 1599-1606 8 045F 590 |
| allfields_unstemmed |
10.1016/j.theriogenology.2016.05.020 doi GBVA2016002000002.pica (DE-627)ELV029433614 (ELSEVIER)S0093-691X(16)30220-5 DE-627 ger DE-627 rakwb eng 590 590 DE-600 070 004 VZ LING DE-30 fid 54.00 bkl 53.71 bkl Patel, M.K. verfasserin aut A 31-kDa seminal plasma heparin–binding protein reduces cold shock stress during cryopreservation of cross-bred cattle bull semen 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In the present study, a 31-kDa protein, purified from cattle bull seminal plasma heparin–binding proteins (SP-HBP), was characterized by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and mass spectrometry. Raw semen of six cross-bred bulls was treated with 31-kDa HBP before cryopreservation to observe its effect on motility, viability, hypo-osmotic swelling test, acrosome integrity, in vitro capacitation/acrosome reaction, and oxidative stress at pre-freeze and frozen–thawed phases of cryopreservation. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis of 31-kDa protein eluted and purified from SP-HBP (separated on acrylamide gels) resulted in a single band of 40 kDa. In matrix-assisted laser desorption/ionization–time of flight analysis, 12 peptides were identified with matching significantly (P < 0.05) to interlukin-6 of bovine with a top score of 55. Addition of 25 μg/mL of fluorescein isothiocyanate–conjugated 31-kDa protein to raw semen and incubation at 37 °C for 20 minutes before cryopreservation resulted in its binding mainly to head region. Treatment of semen with 31-kDa HBP resulted in a significant (P < 0.05) average increase of 9.2%, 6.8%, and 11.7% and 5.5%, 6.5%, and 11.0% in motile, viable, hypo-osmotic swelling–responsive spermatozoa in six bulls at pre-freeze and frozen–thawed phases of cryopreservation, respectively. Percentage of spermatozoa with intact acrosomes nonsignificantly enhanced in the semen treated with 31-kDa HBP at both phases of cryopreservation. An average nonsignificant increase of 3.1% in in vitro capacitated and acrosome-reacted spermatozoa was obtained in semen supplemented with 31-kDa HBP. Addition of 31-kDa HBP also nonsignificantly reduced Malonadialdehyde (MDA) level by 10.7 and 19.3 μM/109 spermatozoa in prefrozen and frozen–thawed semen, respectively. The results obtained here indicate to conclude that treatment of cross-bred cattle bull semen with 31-kDa HBP protects the spermatozoa from cold shock effect by coating the sperm surface. In the present study, a 31-kDa protein, purified from cattle bull seminal plasma heparin–binding proteins (SP-HBP), was characterized by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and mass spectrometry. Raw semen of six cross-bred bulls was treated with 31-kDa HBP before cryopreservation to observe its effect on motility, viability, hypo-osmotic swelling test, acrosome integrity, in vitro capacitation/acrosome reaction, and oxidative stress at pre-freeze and frozen–thawed phases of cryopreservation. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis of 31-kDa protein eluted and purified from SP-HBP (separated on acrylamide gels) resulted in a single band of 40 kDa. In matrix-assisted laser desorption/ionization–time of flight analysis, 12 peptides were identified with matching significantly (P < 0.05) to interlukin-6 of bovine with a top score of 55. Addition of 25 μg/mL of fluorescein isothiocyanate–conjugated 31-kDa protein to raw semen and incubation at 37 °C for 20 minutes before cryopreservation resulted in its binding mainly to head region. Treatment of semen with 31-kDa HBP resulted in a significant (P < 0.05) average increase of 9.2%, 6.8%, and 11.7% and 5.5%, 6.5%, and 11.0% in motile, viable, hypo-osmotic swelling–responsive spermatozoa in six bulls at pre-freeze and frozen–thawed phases of cryopreservation, respectively. Percentage of spermatozoa with intact acrosomes nonsignificantly enhanced in the semen treated with 31-kDa HBP at both phases of cryopreservation. An average nonsignificant increase of 3.1% in in vitro capacitated and acrosome-reacted spermatozoa was obtained in semen supplemented with 31-kDa HBP. Addition of 31-kDa HBP also nonsignificantly reduced Malonadialdehyde (MDA) level by 10.7 and 19.3 μM/109 spermatozoa in prefrozen and frozen–thawed semen, respectively. The results obtained here indicate to conclude that treatment of cross-bred cattle bull semen with 31-kDa HBP protects the spermatozoa from cold shock effect by coating the sperm surface. semen Elsevier 31 kDa Elsevier cattle bull Elsevier SP-HBP Elsevier cold shock stress Elsevier Cheema, R.S. oth Bansal, A.K. oth Gandotra, V.K. oth Enthalten in Elsevier Science Chen, Anyi ELSEVIER Multi-source monitoring information fusion method for dam health diagnosis based on Wasserstein distance 2023 an international journal of animal reproduction Amsterdam [u.a.] (DE-627)ELV009476539 volume:86 year:2016 number:6 day:1 month:10 pages:1599-1606 extent:8 https://doi.org/10.1016/j.theriogenology.2016.05.020 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-LING SSG-OPC-BBI 54.00 Informatik: Allgemeines VZ 53.71 Theoretische Nachrichtentechnik VZ AR 86 2016 6 1 1001 1599-1606 8 045F 590 |
| allfieldsGer |
10.1016/j.theriogenology.2016.05.020 doi GBVA2016002000002.pica (DE-627)ELV029433614 (ELSEVIER)S0093-691X(16)30220-5 DE-627 ger DE-627 rakwb eng 590 590 DE-600 070 004 VZ LING DE-30 fid 54.00 bkl 53.71 bkl Patel, M.K. verfasserin aut A 31-kDa seminal plasma heparin–binding protein reduces cold shock stress during cryopreservation of cross-bred cattle bull semen 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In the present study, a 31-kDa protein, purified from cattle bull seminal plasma heparin–binding proteins (SP-HBP), was characterized by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and mass spectrometry. Raw semen of six cross-bred bulls was treated with 31-kDa HBP before cryopreservation to observe its effect on motility, viability, hypo-osmotic swelling test, acrosome integrity, in vitro capacitation/acrosome reaction, and oxidative stress at pre-freeze and frozen–thawed phases of cryopreservation. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis of 31-kDa protein eluted and purified from SP-HBP (separated on acrylamide gels) resulted in a single band of 40 kDa. In matrix-assisted laser desorption/ionization–time of flight analysis, 12 peptides were identified with matching significantly (P < 0.05) to interlukin-6 of bovine with a top score of 55. Addition of 25 μg/mL of fluorescein isothiocyanate–conjugated 31-kDa protein to raw semen and incubation at 37 °C for 20 minutes before cryopreservation resulted in its binding mainly to head region. Treatment of semen with 31-kDa HBP resulted in a significant (P < 0.05) average increase of 9.2%, 6.8%, and 11.7% and 5.5%, 6.5%, and 11.0% in motile, viable, hypo-osmotic swelling–responsive spermatozoa in six bulls at pre-freeze and frozen–thawed phases of cryopreservation, respectively. Percentage of spermatozoa with intact acrosomes nonsignificantly enhanced in the semen treated with 31-kDa HBP at both phases of cryopreservation. An average nonsignificant increase of 3.1% in in vitro capacitated and acrosome-reacted spermatozoa was obtained in semen supplemented with 31-kDa HBP. Addition of 31-kDa HBP also nonsignificantly reduced Malonadialdehyde (MDA) level by 10.7 and 19.3 μM/109 spermatozoa in prefrozen and frozen–thawed semen, respectively. The results obtained here indicate to conclude that treatment of cross-bred cattle bull semen with 31-kDa HBP protects the spermatozoa from cold shock effect by coating the sperm surface. In the present study, a 31-kDa protein, purified from cattle bull seminal plasma heparin–binding proteins (SP-HBP), was characterized by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and mass spectrometry. Raw semen of six cross-bred bulls was treated with 31-kDa HBP before cryopreservation to observe its effect on motility, viability, hypo-osmotic swelling test, acrosome integrity, in vitro capacitation/acrosome reaction, and oxidative stress at pre-freeze and frozen–thawed phases of cryopreservation. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis of 31-kDa protein eluted and purified from SP-HBP (separated on acrylamide gels) resulted in a single band of 40 kDa. In matrix-assisted laser desorption/ionization–time of flight analysis, 12 peptides were identified with matching significantly (P < 0.05) to interlukin-6 of bovine with a top score of 55. Addition of 25 μg/mL of fluorescein isothiocyanate–conjugated 31-kDa protein to raw semen and incubation at 37 °C for 20 minutes before cryopreservation resulted in its binding mainly to head region. Treatment of semen with 31-kDa HBP resulted in a significant (P < 0.05) average increase of 9.2%, 6.8%, and 11.7% and 5.5%, 6.5%, and 11.0% in motile, viable, hypo-osmotic swelling–responsive spermatozoa in six bulls at pre-freeze and frozen–thawed phases of cryopreservation, respectively. Percentage of spermatozoa with intact acrosomes nonsignificantly enhanced in the semen treated with 31-kDa HBP at both phases of cryopreservation. An average nonsignificant increase of 3.1% in in vitro capacitated and acrosome-reacted spermatozoa was obtained in semen supplemented with 31-kDa HBP. Addition of 31-kDa HBP also nonsignificantly reduced Malonadialdehyde (MDA) level by 10.7 and 19.3 μM/109 spermatozoa in prefrozen and frozen–thawed semen, respectively. The results obtained here indicate to conclude that treatment of cross-bred cattle bull semen with 31-kDa HBP protects the spermatozoa from cold shock effect by coating the sperm surface. semen Elsevier 31 kDa Elsevier cattle bull Elsevier SP-HBP Elsevier cold shock stress Elsevier Cheema, R.S. oth Bansal, A.K. oth Gandotra, V.K. oth Enthalten in Elsevier Science Chen, Anyi ELSEVIER Multi-source monitoring information fusion method for dam health diagnosis based on Wasserstein distance 2023 an international journal of animal reproduction Amsterdam [u.a.] (DE-627)ELV009476539 volume:86 year:2016 number:6 day:1 month:10 pages:1599-1606 extent:8 https://doi.org/10.1016/j.theriogenology.2016.05.020 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-LING SSG-OPC-BBI 54.00 Informatik: Allgemeines VZ 53.71 Theoretische Nachrichtentechnik VZ AR 86 2016 6 1 1001 1599-1606 8 045F 590 |
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10.1016/j.theriogenology.2016.05.020 doi GBVA2016002000002.pica (DE-627)ELV029433614 (ELSEVIER)S0093-691X(16)30220-5 DE-627 ger DE-627 rakwb eng 590 590 DE-600 070 004 VZ LING DE-30 fid 54.00 bkl 53.71 bkl Patel, M.K. verfasserin aut A 31-kDa seminal plasma heparin–binding protein reduces cold shock stress during cryopreservation of cross-bred cattle bull semen 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In the present study, a 31-kDa protein, purified from cattle bull seminal plasma heparin–binding proteins (SP-HBP), was characterized by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and mass spectrometry. Raw semen of six cross-bred bulls was treated with 31-kDa HBP before cryopreservation to observe its effect on motility, viability, hypo-osmotic swelling test, acrosome integrity, in vitro capacitation/acrosome reaction, and oxidative stress at pre-freeze and frozen–thawed phases of cryopreservation. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis of 31-kDa protein eluted and purified from SP-HBP (separated on acrylamide gels) resulted in a single band of 40 kDa. In matrix-assisted laser desorption/ionization–time of flight analysis, 12 peptides were identified with matching significantly (P < 0.05) to interlukin-6 of bovine with a top score of 55. Addition of 25 μg/mL of fluorescein isothiocyanate–conjugated 31-kDa protein to raw semen and incubation at 37 °C for 20 minutes before cryopreservation resulted in its binding mainly to head region. Treatment of semen with 31-kDa HBP resulted in a significant (P < 0.05) average increase of 9.2%, 6.8%, and 11.7% and 5.5%, 6.5%, and 11.0% in motile, viable, hypo-osmotic swelling–responsive spermatozoa in six bulls at pre-freeze and frozen–thawed phases of cryopreservation, respectively. Percentage of spermatozoa with intact acrosomes nonsignificantly enhanced in the semen treated with 31-kDa HBP at both phases of cryopreservation. An average nonsignificant increase of 3.1% in in vitro capacitated and acrosome-reacted spermatozoa was obtained in semen supplemented with 31-kDa HBP. Addition of 31-kDa HBP also nonsignificantly reduced Malonadialdehyde (MDA) level by 10.7 and 19.3 μM/109 spermatozoa in prefrozen and frozen–thawed semen, respectively. The results obtained here indicate to conclude that treatment of cross-bred cattle bull semen with 31-kDa HBP protects the spermatozoa from cold shock effect by coating the sperm surface. In the present study, a 31-kDa protein, purified from cattle bull seminal plasma heparin–binding proteins (SP-HBP), was characterized by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and mass spectrometry. Raw semen of six cross-bred bulls was treated with 31-kDa HBP before cryopreservation to observe its effect on motility, viability, hypo-osmotic swelling test, acrosome integrity, in vitro capacitation/acrosome reaction, and oxidative stress at pre-freeze and frozen–thawed phases of cryopreservation. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis of 31-kDa protein eluted and purified from SP-HBP (separated on acrylamide gels) resulted in a single band of 40 kDa. In matrix-assisted laser desorption/ionization–time of flight analysis, 12 peptides were identified with matching significantly (P < 0.05) to interlukin-6 of bovine with a top score of 55. Addition of 25 μg/mL of fluorescein isothiocyanate–conjugated 31-kDa protein to raw semen and incubation at 37 °C for 20 minutes before cryopreservation resulted in its binding mainly to head region. Treatment of semen with 31-kDa HBP resulted in a significant (P < 0.05) average increase of 9.2%, 6.8%, and 11.7% and 5.5%, 6.5%, and 11.0% in motile, viable, hypo-osmotic swelling–responsive spermatozoa in six bulls at pre-freeze and frozen–thawed phases of cryopreservation, respectively. Percentage of spermatozoa with intact acrosomes nonsignificantly enhanced in the semen treated with 31-kDa HBP at both phases of cryopreservation. An average nonsignificant increase of 3.1% in in vitro capacitated and acrosome-reacted spermatozoa was obtained in semen supplemented with 31-kDa HBP. Addition of 31-kDa HBP also nonsignificantly reduced Malonadialdehyde (MDA) level by 10.7 and 19.3 μM/109 spermatozoa in prefrozen and frozen–thawed semen, respectively. The results obtained here indicate to conclude that treatment of cross-bred cattle bull semen with 31-kDa HBP protects the spermatozoa from cold shock effect by coating the sperm surface. semen Elsevier 31 kDa Elsevier cattle bull Elsevier SP-HBP Elsevier cold shock stress Elsevier Cheema, R.S. oth Bansal, A.K. oth Gandotra, V.K. oth Enthalten in Elsevier Science Chen, Anyi ELSEVIER Multi-source monitoring information fusion method for dam health diagnosis based on Wasserstein distance 2023 an international journal of animal reproduction Amsterdam [u.a.] (DE-627)ELV009476539 volume:86 year:2016 number:6 day:1 month:10 pages:1599-1606 extent:8 https://doi.org/10.1016/j.theriogenology.2016.05.020 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-LING SSG-OPC-BBI 54.00 Informatik: Allgemeines VZ 53.71 Theoretische Nachrichtentechnik VZ AR 86 2016 6 1 1001 1599-1606 8 045F 590 |
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a 31-kda seminal plasma heparin–binding protein reduces cold shock stress during cryopreservation of cross-bred cattle bull semen |
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A 31-kDa seminal plasma heparin–binding protein reduces cold shock stress during cryopreservation of cross-bred cattle bull semen |
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In the present study, a 31-kDa protein, purified from cattle bull seminal plasma heparin–binding proteins (SP-HBP), was characterized by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and mass spectrometry. Raw semen of six cross-bred bulls was treated with 31-kDa HBP before cryopreservation to observe its effect on motility, viability, hypo-osmotic swelling test, acrosome integrity, in vitro capacitation/acrosome reaction, and oxidative stress at pre-freeze and frozen–thawed phases of cryopreservation. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis of 31-kDa protein eluted and purified from SP-HBP (separated on acrylamide gels) resulted in a single band of 40 kDa. In matrix-assisted laser desorption/ionization–time of flight analysis, 12 peptides were identified with matching significantly (P < 0.05) to interlukin-6 of bovine with a top score of 55. Addition of 25 μg/mL of fluorescein isothiocyanate–conjugated 31-kDa protein to raw semen and incubation at 37 °C for 20 minutes before cryopreservation resulted in its binding mainly to head region. Treatment of semen with 31-kDa HBP resulted in a significant (P < 0.05) average increase of 9.2%, 6.8%, and 11.7% and 5.5%, 6.5%, and 11.0% in motile, viable, hypo-osmotic swelling–responsive spermatozoa in six bulls at pre-freeze and frozen–thawed phases of cryopreservation, respectively. Percentage of spermatozoa with intact acrosomes nonsignificantly enhanced in the semen treated with 31-kDa HBP at both phases of cryopreservation. An average nonsignificant increase of 3.1% in in vitro capacitated and acrosome-reacted spermatozoa was obtained in semen supplemented with 31-kDa HBP. Addition of 31-kDa HBP also nonsignificantly reduced Malonadialdehyde (MDA) level by 10.7 and 19.3 μM/109 spermatozoa in prefrozen and frozen–thawed semen, respectively. The results obtained here indicate to conclude that treatment of cross-bred cattle bull semen with 31-kDa HBP protects the spermatozoa from cold shock effect by coating the sperm surface. |
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In the present study, a 31-kDa protein, purified from cattle bull seminal plasma heparin–binding proteins (SP-HBP), was characterized by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and mass spectrometry. Raw semen of six cross-bred bulls was treated with 31-kDa HBP before cryopreservation to observe its effect on motility, viability, hypo-osmotic swelling test, acrosome integrity, in vitro capacitation/acrosome reaction, and oxidative stress at pre-freeze and frozen–thawed phases of cryopreservation. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis of 31-kDa protein eluted and purified from SP-HBP (separated on acrylamide gels) resulted in a single band of 40 kDa. In matrix-assisted laser desorption/ionization–time of flight analysis, 12 peptides were identified with matching significantly (P < 0.05) to interlukin-6 of bovine with a top score of 55. Addition of 25 μg/mL of fluorescein isothiocyanate–conjugated 31-kDa protein to raw semen and incubation at 37 °C for 20 minutes before cryopreservation resulted in its binding mainly to head region. Treatment of semen with 31-kDa HBP resulted in a significant (P < 0.05) average increase of 9.2%, 6.8%, and 11.7% and 5.5%, 6.5%, and 11.0% in motile, viable, hypo-osmotic swelling–responsive spermatozoa in six bulls at pre-freeze and frozen–thawed phases of cryopreservation, respectively. Percentage of spermatozoa with intact acrosomes nonsignificantly enhanced in the semen treated with 31-kDa HBP at both phases of cryopreservation. An average nonsignificant increase of 3.1% in in vitro capacitated and acrosome-reacted spermatozoa was obtained in semen supplemented with 31-kDa HBP. Addition of 31-kDa HBP also nonsignificantly reduced Malonadialdehyde (MDA) level by 10.7 and 19.3 μM/109 spermatozoa in prefrozen and frozen–thawed semen, respectively. The results obtained here indicate to conclude that treatment of cross-bred cattle bull semen with 31-kDa HBP protects the spermatozoa from cold shock effect by coating the sperm surface. |
| abstract_unstemmed |
In the present study, a 31-kDa protein, purified from cattle bull seminal plasma heparin–binding proteins (SP-HBP), was characterized by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and mass spectrometry. Raw semen of six cross-bred bulls was treated with 31-kDa HBP before cryopreservation to observe its effect on motility, viability, hypo-osmotic swelling test, acrosome integrity, in vitro capacitation/acrosome reaction, and oxidative stress at pre-freeze and frozen–thawed phases of cryopreservation. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis of 31-kDa protein eluted and purified from SP-HBP (separated on acrylamide gels) resulted in a single band of 40 kDa. In matrix-assisted laser desorption/ionization–time of flight analysis, 12 peptides were identified with matching significantly (P < 0.05) to interlukin-6 of bovine with a top score of 55. Addition of 25 μg/mL of fluorescein isothiocyanate–conjugated 31-kDa protein to raw semen and incubation at 37 °C for 20 minutes before cryopreservation resulted in its binding mainly to head region. Treatment of semen with 31-kDa HBP resulted in a significant (P < 0.05) average increase of 9.2%, 6.8%, and 11.7% and 5.5%, 6.5%, and 11.0% in motile, viable, hypo-osmotic swelling–responsive spermatozoa in six bulls at pre-freeze and frozen–thawed phases of cryopreservation, respectively. Percentage of spermatozoa with intact acrosomes nonsignificantly enhanced in the semen treated with 31-kDa HBP at both phases of cryopreservation. An average nonsignificant increase of 3.1% in in vitro capacitated and acrosome-reacted spermatozoa was obtained in semen supplemented with 31-kDa HBP. Addition of 31-kDa HBP also nonsignificantly reduced Malonadialdehyde (MDA) level by 10.7 and 19.3 μM/109 spermatozoa in prefrozen and frozen–thawed semen, respectively. The results obtained here indicate to conclude that treatment of cross-bred cattle bull semen with 31-kDa HBP protects the spermatozoa from cold shock effect by coating the sperm surface. |
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A 31-kDa seminal plasma heparin–binding protein reduces cold shock stress during cryopreservation of cross-bred cattle bull semen |
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https://doi.org/10.1016/j.theriogenology.2016.05.020 |
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Cheema, R.S. Bansal, A.K. Gandotra, V.K. |
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10.1016/j.theriogenology.2016.05.020 |
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