Expression and characterization of two tyrosinases from the trematode Schistosoma japonicum
Abstract Tyrosinase (TYR) was thought to play a critical role during trematode egg production. In this study, we analyzed two genes (SjTYR1 and SjTYR2), derived from Schistosoma japonicum genome databases, which encode proteins with significant homologies to mammalian TYR. They exhibited the typical...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Cai, Guobin [verfasserIn] Bae, Youngan [verfasserIn] Zhang, Ying [verfasserIn] He, Yuan [verfasserIn] Jiang, Mingsen [verfasserIn] He, Li [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2008 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Parasitology research - Berlin : Springer, 1928, 104(2008), 3 vom: 30. Okt. |
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| Übergeordnetes Werk: |
volume:104 ; year:2008 ; number:3 ; day:30 ; month:10 |
| Links: |
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| DOI / URN: |
10.1007/s00436-008-1236-5 |
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| Katalog-ID: |
SPR005905311 |
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| 100 | 1 | |a Cai, Guobin |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Expression and characterization of two tyrosinases from the trematode Schistosoma japonicum |
| 264 | 1 | |c 2008 | |
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| 520 | |a Abstract Tyrosinase (TYR) was thought to play a critical role during trematode egg production. In this study, we analyzed two genes (SjTYR1 and SjTYR2), derived from Schistosoma japonicum genome databases, which encode proteins with significant homologies to mammalian TYR. They exhibited the typical TYR topology, including two copper-binding domains and a highly conserved cysteine-rich domain. Semi-quantitative reverse transcription polymerase chain reaction showed that two SjTYR genes were mainly expressed in the female adult worm. A complementary DNA coding the putative common copper center domain of each SjTYR was cloned and inserted into a pET-28a-c(+) prokaryotic expression vector. After purification, the recombinant proteins expressed in Escherichia coli were used to produce their specific antibodies. The native active SjTYRs enzyme appeared to function as a homodimer, the subunits of which were linked to each other via covalent disulfide bonds. Both female and male worms possessed monophenol oxidase and diphenol oxidase activities of TYR. The relative enzymatic activities were 0.165 $ min^{−1} $ $ mg^{−1} $ and 0.0805 $ min^{−1} $ $ mg^{−1} $, which were inhibited by a copper-chelating agent (allyl thiourea) and correlated with disruption of female egg production. Our results revealed that SjTYRs might play a significant role during eggshell formation. | ||
| 650 | 4 | |a Adult Worm |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Female Worm |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Schistosoma Japonicum |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Phenol Oxidase Activity |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Male Worm |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Bae, Youngan |e verfasserin |4 aut | |
| 700 | 1 | |a Zhang, Ying |e verfasserin |4 aut | |
| 700 | 1 | |a He, Yuan |e verfasserin |4 aut | |
| 700 | 1 | |a Jiang, Mingsen |e verfasserin |4 aut | |
| 700 | 1 | |a He, Li |e verfasserin |4 aut | |
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| 773 | 1 | 8 | |g volume:104 |g year:2008 |g number:3 |g day:30 |g month:10 |
| 856 | 4 | 0 | |u https://dx.doi.org/10.1007/s00436-008-1236-5 |z lizenzpflichtig |3 Volltext |
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| 912 | |a GBV_ILN_2014 | ||
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| 912 | |a GBV_ILN_2049 | ||
| 912 | |a GBV_ILN_2050 | ||
| 912 | |a GBV_ILN_2055 | ||
| 912 | |a GBV_ILN_2057 | ||
| 912 | |a GBV_ILN_2059 | ||
| 912 | |a GBV_ILN_2061 | ||
| 912 | |a GBV_ILN_2064 | ||
| 912 | |a GBV_ILN_2065 | ||
| 912 | |a GBV_ILN_2068 | ||
| 912 | |a GBV_ILN_2070 | ||
| 912 | |a GBV_ILN_2086 | ||
| 912 | |a GBV_ILN_2088 | ||
| 912 | |a GBV_ILN_2093 | ||
| 912 | |a GBV_ILN_2106 | ||
| 912 | |a GBV_ILN_2107 | ||
| 912 | |a GBV_ILN_2108 | ||
| 912 | |a GBV_ILN_2110 | ||
| 912 | |a GBV_ILN_2111 | ||
| 912 | |a GBV_ILN_2112 | ||
| 912 | |a GBV_ILN_2113 | ||
| 912 | |a GBV_ILN_2116 | ||
| 912 | |a GBV_ILN_2118 | ||
| 912 | |a GBV_ILN_2119 | ||
| 912 | |a GBV_ILN_2122 | ||
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| 912 | |a GBV_ILN_2148 | ||
| 912 | |a GBV_ILN_2152 | ||
| 912 | |a GBV_ILN_2153 | ||
| 912 | |a GBV_ILN_2188 | ||
| 912 | |a GBV_ILN_2190 | ||
| 912 | |a GBV_ILN_2232 | ||
| 912 | |a GBV_ILN_2336 | ||
| 912 | |a GBV_ILN_2446 | ||
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| 912 | |a GBV_ILN_4035 | ||
| 912 | |a GBV_ILN_4037 | ||
| 912 | |a GBV_ILN_4046 | ||
| 912 | |a GBV_ILN_4112 | ||
| 912 | |a GBV_ILN_4125 | ||
| 912 | |a GBV_ILN_4126 | ||
| 912 | |a GBV_ILN_4242 | ||
| 912 | |a GBV_ILN_4246 | ||
| 912 | |a GBV_ILN_4249 | ||
| 912 | |a GBV_ILN_4251 | ||
| 912 | |a GBV_ILN_4305 | ||
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| 912 | |a GBV_ILN_4307 | ||
| 912 | |a GBV_ILN_4313 | ||
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| 912 | |a GBV_ILN_4323 | ||
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| 912 | |a GBV_ILN_4326 | ||
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| allfields |
10.1007/s00436-008-1236-5 doi (DE-627)SPR005905311 (SPR)s00436-008-1236-5-e DE-627 ger DE-627 rakwb eng 590 610 ASE 44.44 bkl 42.00 bkl Cai, Guobin verfasserin aut Expression and characterization of two tyrosinases from the trematode Schistosoma japonicum 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Tyrosinase (TYR) was thought to play a critical role during trematode egg production. In this study, we analyzed two genes (SjTYR1 and SjTYR2), derived from Schistosoma japonicum genome databases, which encode proteins with significant homologies to mammalian TYR. They exhibited the typical TYR topology, including two copper-binding domains and a highly conserved cysteine-rich domain. Semi-quantitative reverse transcription polymerase chain reaction showed that two SjTYR genes were mainly expressed in the female adult worm. A complementary DNA coding the putative common copper center domain of each SjTYR was cloned and inserted into a pET-28a-c(+) prokaryotic expression vector. After purification, the recombinant proteins expressed in Escherichia coli were used to produce their specific antibodies. The native active SjTYRs enzyme appeared to function as a homodimer, the subunits of which were linked to each other via covalent disulfide bonds. Both female and male worms possessed monophenol oxidase and diphenol oxidase activities of TYR. The relative enzymatic activities were 0.165 $ min^{−1} $ $ mg^{−1} $ and 0.0805 $ min^{−1} $ $ mg^{−1} $, which were inhibited by a copper-chelating agent (allyl thiourea) and correlated with disruption of female egg production. Our results revealed that SjTYRs might play a significant role during eggshell formation. Adult Worm (dpeaa)DE-He213 Female Worm (dpeaa)DE-He213 Schistosoma Japonicum (dpeaa)DE-He213 Phenol Oxidase Activity (dpeaa)DE-He213 Male Worm (dpeaa)DE-He213 Bae, Youngan verfasserin aut Zhang, Ying verfasserin aut He, Yuan verfasserin aut Jiang, Mingsen verfasserin aut He, Li verfasserin aut Enthalten in Parasitology research Berlin : Springer, 1928 104(2008), 3 vom: 30. Okt. (DE-627)254638627 (DE-600)1462976-8 1432-1955 nnns volume:104 year:2008 number:3 day:30 month:10 https://dx.doi.org/10.1007/s00436-008-1236-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.44 ASE 42.00 ASE AR 104 2008 3 30 10 |
| spelling |
10.1007/s00436-008-1236-5 doi (DE-627)SPR005905311 (SPR)s00436-008-1236-5-e DE-627 ger DE-627 rakwb eng 590 610 ASE 44.44 bkl 42.00 bkl Cai, Guobin verfasserin aut Expression and characterization of two tyrosinases from the trematode Schistosoma japonicum 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Tyrosinase (TYR) was thought to play a critical role during trematode egg production. In this study, we analyzed two genes (SjTYR1 and SjTYR2), derived from Schistosoma japonicum genome databases, which encode proteins with significant homologies to mammalian TYR. They exhibited the typical TYR topology, including two copper-binding domains and a highly conserved cysteine-rich domain. Semi-quantitative reverse transcription polymerase chain reaction showed that two SjTYR genes were mainly expressed in the female adult worm. A complementary DNA coding the putative common copper center domain of each SjTYR was cloned and inserted into a pET-28a-c(+) prokaryotic expression vector. After purification, the recombinant proteins expressed in Escherichia coli were used to produce their specific antibodies. The native active SjTYRs enzyme appeared to function as a homodimer, the subunits of which were linked to each other via covalent disulfide bonds. Both female and male worms possessed monophenol oxidase and diphenol oxidase activities of TYR. The relative enzymatic activities were 0.165 $ min^{−1} $ $ mg^{−1} $ and 0.0805 $ min^{−1} $ $ mg^{−1} $, which were inhibited by a copper-chelating agent (allyl thiourea) and correlated with disruption of female egg production. Our results revealed that SjTYRs might play a significant role during eggshell formation. Adult Worm (dpeaa)DE-He213 Female Worm (dpeaa)DE-He213 Schistosoma Japonicum (dpeaa)DE-He213 Phenol Oxidase Activity (dpeaa)DE-He213 Male Worm (dpeaa)DE-He213 Bae, Youngan verfasserin aut Zhang, Ying verfasserin aut He, Yuan verfasserin aut Jiang, Mingsen verfasserin aut He, Li verfasserin aut Enthalten in Parasitology research Berlin : Springer, 1928 104(2008), 3 vom: 30. Okt. (DE-627)254638627 (DE-600)1462976-8 1432-1955 nnns volume:104 year:2008 number:3 day:30 month:10 https://dx.doi.org/10.1007/s00436-008-1236-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.44 ASE 42.00 ASE AR 104 2008 3 30 10 |
| allfields_unstemmed |
10.1007/s00436-008-1236-5 doi (DE-627)SPR005905311 (SPR)s00436-008-1236-5-e DE-627 ger DE-627 rakwb eng 590 610 ASE 44.44 bkl 42.00 bkl Cai, Guobin verfasserin aut Expression and characterization of two tyrosinases from the trematode Schistosoma japonicum 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Tyrosinase (TYR) was thought to play a critical role during trematode egg production. In this study, we analyzed two genes (SjTYR1 and SjTYR2), derived from Schistosoma japonicum genome databases, which encode proteins with significant homologies to mammalian TYR. They exhibited the typical TYR topology, including two copper-binding domains and a highly conserved cysteine-rich domain. Semi-quantitative reverse transcription polymerase chain reaction showed that two SjTYR genes were mainly expressed in the female adult worm. A complementary DNA coding the putative common copper center domain of each SjTYR was cloned and inserted into a pET-28a-c(+) prokaryotic expression vector. After purification, the recombinant proteins expressed in Escherichia coli were used to produce their specific antibodies. The native active SjTYRs enzyme appeared to function as a homodimer, the subunits of which were linked to each other via covalent disulfide bonds. Both female and male worms possessed monophenol oxidase and diphenol oxidase activities of TYR. The relative enzymatic activities were 0.165 $ min^{−1} $ $ mg^{−1} $ and 0.0805 $ min^{−1} $ $ mg^{−1} $, which were inhibited by a copper-chelating agent (allyl thiourea) and correlated with disruption of female egg production. Our results revealed that SjTYRs might play a significant role during eggshell formation. Adult Worm (dpeaa)DE-He213 Female Worm (dpeaa)DE-He213 Schistosoma Japonicum (dpeaa)DE-He213 Phenol Oxidase Activity (dpeaa)DE-He213 Male Worm (dpeaa)DE-He213 Bae, Youngan verfasserin aut Zhang, Ying verfasserin aut He, Yuan verfasserin aut Jiang, Mingsen verfasserin aut He, Li verfasserin aut Enthalten in Parasitology research Berlin : Springer, 1928 104(2008), 3 vom: 30. Okt. (DE-627)254638627 (DE-600)1462976-8 1432-1955 nnns volume:104 year:2008 number:3 day:30 month:10 https://dx.doi.org/10.1007/s00436-008-1236-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.44 ASE 42.00 ASE AR 104 2008 3 30 10 |
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10.1007/s00436-008-1236-5 doi (DE-627)SPR005905311 (SPR)s00436-008-1236-5-e DE-627 ger DE-627 rakwb eng 590 610 ASE 44.44 bkl 42.00 bkl Cai, Guobin verfasserin aut Expression and characterization of two tyrosinases from the trematode Schistosoma japonicum 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Tyrosinase (TYR) was thought to play a critical role during trematode egg production. In this study, we analyzed two genes (SjTYR1 and SjTYR2), derived from Schistosoma japonicum genome databases, which encode proteins with significant homologies to mammalian TYR. They exhibited the typical TYR topology, including two copper-binding domains and a highly conserved cysteine-rich domain. Semi-quantitative reverse transcription polymerase chain reaction showed that two SjTYR genes were mainly expressed in the female adult worm. A complementary DNA coding the putative common copper center domain of each SjTYR was cloned and inserted into a pET-28a-c(+) prokaryotic expression vector. After purification, the recombinant proteins expressed in Escherichia coli were used to produce their specific antibodies. The native active SjTYRs enzyme appeared to function as a homodimer, the subunits of which were linked to each other via covalent disulfide bonds. Both female and male worms possessed monophenol oxidase and diphenol oxidase activities of TYR. The relative enzymatic activities were 0.165 $ min^{−1} $ $ mg^{−1} $ and 0.0805 $ min^{−1} $ $ mg^{−1} $, which were inhibited by a copper-chelating agent (allyl thiourea) and correlated with disruption of female egg production. Our results revealed that SjTYRs might play a significant role during eggshell formation. Adult Worm (dpeaa)DE-He213 Female Worm (dpeaa)DE-He213 Schistosoma Japonicum (dpeaa)DE-He213 Phenol Oxidase Activity (dpeaa)DE-He213 Male Worm (dpeaa)DE-He213 Bae, Youngan verfasserin aut Zhang, Ying verfasserin aut He, Yuan verfasserin aut Jiang, Mingsen verfasserin aut He, Li verfasserin aut Enthalten in Parasitology research Berlin : Springer, 1928 104(2008), 3 vom: 30. Okt. (DE-627)254638627 (DE-600)1462976-8 1432-1955 nnns volume:104 year:2008 number:3 day:30 month:10 https://dx.doi.org/10.1007/s00436-008-1236-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.44 ASE 42.00 ASE AR 104 2008 3 30 10 |
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10.1007/s00436-008-1236-5 doi (DE-627)SPR005905311 (SPR)s00436-008-1236-5-e DE-627 ger DE-627 rakwb eng 590 610 ASE 44.44 bkl 42.00 bkl Cai, Guobin verfasserin aut Expression and characterization of two tyrosinases from the trematode Schistosoma japonicum 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Tyrosinase (TYR) was thought to play a critical role during trematode egg production. In this study, we analyzed two genes (SjTYR1 and SjTYR2), derived from Schistosoma japonicum genome databases, which encode proteins with significant homologies to mammalian TYR. They exhibited the typical TYR topology, including two copper-binding domains and a highly conserved cysteine-rich domain. Semi-quantitative reverse transcription polymerase chain reaction showed that two SjTYR genes were mainly expressed in the female adult worm. A complementary DNA coding the putative common copper center domain of each SjTYR was cloned and inserted into a pET-28a-c(+) prokaryotic expression vector. After purification, the recombinant proteins expressed in Escherichia coli were used to produce their specific antibodies. The native active SjTYRs enzyme appeared to function as a homodimer, the subunits of which were linked to each other via covalent disulfide bonds. Both female and male worms possessed monophenol oxidase and diphenol oxidase activities of TYR. The relative enzymatic activities were 0.165 $ min^{−1} $ $ mg^{−1} $ and 0.0805 $ min^{−1} $ $ mg^{−1} $, which were inhibited by a copper-chelating agent (allyl thiourea) and correlated with disruption of female egg production. Our results revealed that SjTYRs might play a significant role during eggshell formation. Adult Worm (dpeaa)DE-He213 Female Worm (dpeaa)DE-He213 Schistosoma Japonicum (dpeaa)DE-He213 Phenol Oxidase Activity (dpeaa)DE-He213 Male Worm (dpeaa)DE-He213 Bae, Youngan verfasserin aut Zhang, Ying verfasserin aut He, Yuan verfasserin aut Jiang, Mingsen verfasserin aut He, Li verfasserin aut Enthalten in Parasitology research Berlin : Springer, 1928 104(2008), 3 vom: 30. Okt. (DE-627)254638627 (DE-600)1462976-8 1432-1955 nnns volume:104 year:2008 number:3 day:30 month:10 https://dx.doi.org/10.1007/s00436-008-1236-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.44 ASE 42.00 ASE AR 104 2008 3 30 10 |
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Enthalten in Parasitology research 104(2008), 3 vom: 30. Okt. volume:104 year:2008 number:3 day:30 month:10 |
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Cai, Guobin @@aut@@ Bae, Youngan @@aut@@ Zhang, Ying @@aut@@ He, Yuan @@aut@@ Jiang, Mingsen @@aut@@ He, Li @@aut@@ |
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In this study, we analyzed two genes (SjTYR1 and SjTYR2), derived from Schistosoma japonicum genome databases, which encode proteins with significant homologies to mammalian TYR. They exhibited the typical TYR topology, including two copper-binding domains and a highly conserved cysteine-rich domain. Semi-quantitative reverse transcription polymerase chain reaction showed that two SjTYR genes were mainly expressed in the female adult worm. A complementary DNA coding the putative common copper center domain of each SjTYR was cloned and inserted into a pET-28a-c(+) prokaryotic expression vector. After purification, the recombinant proteins expressed in Escherichia coli were used to produce their specific antibodies. The native active SjTYRs enzyme appeared to function as a homodimer, the subunits of which were linked to each other via covalent disulfide bonds. Both female and male worms possessed monophenol oxidase and diphenol oxidase activities of TYR. The relative enzymatic activities were 0.165 $ min^{−1} $ $ mg^{−1} $ and 0.0805 $ min^{−1} $ $ mg^{−1} $, which were inhibited by a copper-chelating agent (allyl thiourea) and correlated with disruption of female egg production. 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|
| author |
Cai, Guobin |
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Cai, Guobin ddc 590 bkl 44.44 bkl 42.00 misc Adult Worm misc Female Worm misc Schistosoma Japonicum misc Phenol Oxidase Activity misc Male Worm Expression and characterization of two tyrosinases from the trematode Schistosoma japonicum |
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590 610 ASE 44.44 bkl 42.00 bkl Expression and characterization of two tyrosinases from the trematode Schistosoma japonicum Adult Worm (dpeaa)DE-He213 Female Worm (dpeaa)DE-He213 Schistosoma Japonicum (dpeaa)DE-He213 Phenol Oxidase Activity (dpeaa)DE-He213 Male Worm (dpeaa)DE-He213 |
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ddc 590 bkl 44.44 bkl 42.00 misc Adult Worm misc Female Worm misc Schistosoma Japonicum misc Phenol Oxidase Activity misc Male Worm |
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ddc 590 bkl 44.44 bkl 42.00 misc Adult Worm misc Female Worm misc Schistosoma Japonicum misc Phenol Oxidase Activity misc Male Worm |
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ddc 590 bkl 44.44 bkl 42.00 misc Adult Worm misc Female Worm misc Schistosoma Japonicum misc Phenol Oxidase Activity misc Male Worm |
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Expression and characterization of two tyrosinases from the trematode Schistosoma japonicum |
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Expression and characterization of two tyrosinases from the trematode Schistosoma japonicum |
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Cai, Guobin |
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Cai, Guobin Bae, Youngan Zhang, Ying He, Yuan Jiang, Mingsen He, Li |
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expression and characterization of two tyrosinases from the trematode schistosoma japonicum |
| title_auth |
Expression and characterization of two tyrosinases from the trematode Schistosoma japonicum |
| abstract |
Abstract Tyrosinase (TYR) was thought to play a critical role during trematode egg production. In this study, we analyzed two genes (SjTYR1 and SjTYR2), derived from Schistosoma japonicum genome databases, which encode proteins with significant homologies to mammalian TYR. They exhibited the typical TYR topology, including two copper-binding domains and a highly conserved cysteine-rich domain. Semi-quantitative reverse transcription polymerase chain reaction showed that two SjTYR genes were mainly expressed in the female adult worm. A complementary DNA coding the putative common copper center domain of each SjTYR was cloned and inserted into a pET-28a-c(+) prokaryotic expression vector. After purification, the recombinant proteins expressed in Escherichia coli were used to produce their specific antibodies. The native active SjTYRs enzyme appeared to function as a homodimer, the subunits of which were linked to each other via covalent disulfide bonds. Both female and male worms possessed monophenol oxidase and diphenol oxidase activities of TYR. The relative enzymatic activities were 0.165 $ min^{−1} $ $ mg^{−1} $ and 0.0805 $ min^{−1} $ $ mg^{−1} $, which were inhibited by a copper-chelating agent (allyl thiourea) and correlated with disruption of female egg production. Our results revealed that SjTYRs might play a significant role during eggshell formation. |
| abstractGer |
Abstract Tyrosinase (TYR) was thought to play a critical role during trematode egg production. In this study, we analyzed two genes (SjTYR1 and SjTYR2), derived from Schistosoma japonicum genome databases, which encode proteins with significant homologies to mammalian TYR. They exhibited the typical TYR topology, including two copper-binding domains and a highly conserved cysteine-rich domain. Semi-quantitative reverse transcription polymerase chain reaction showed that two SjTYR genes were mainly expressed in the female adult worm. A complementary DNA coding the putative common copper center domain of each SjTYR was cloned and inserted into a pET-28a-c(+) prokaryotic expression vector. After purification, the recombinant proteins expressed in Escherichia coli were used to produce their specific antibodies. The native active SjTYRs enzyme appeared to function as a homodimer, the subunits of which were linked to each other via covalent disulfide bonds. Both female and male worms possessed monophenol oxidase and diphenol oxidase activities of TYR. The relative enzymatic activities were 0.165 $ min^{−1} $ $ mg^{−1} $ and 0.0805 $ min^{−1} $ $ mg^{−1} $, which were inhibited by a copper-chelating agent (allyl thiourea) and correlated with disruption of female egg production. Our results revealed that SjTYRs might play a significant role during eggshell formation. |
| abstract_unstemmed |
Abstract Tyrosinase (TYR) was thought to play a critical role during trematode egg production. In this study, we analyzed two genes (SjTYR1 and SjTYR2), derived from Schistosoma japonicum genome databases, which encode proteins with significant homologies to mammalian TYR. They exhibited the typical TYR topology, including two copper-binding domains and a highly conserved cysteine-rich domain. Semi-quantitative reverse transcription polymerase chain reaction showed that two SjTYR genes were mainly expressed in the female adult worm. A complementary DNA coding the putative common copper center domain of each SjTYR was cloned and inserted into a pET-28a-c(+) prokaryotic expression vector. After purification, the recombinant proteins expressed in Escherichia coli were used to produce their specific antibodies. The native active SjTYRs enzyme appeared to function as a homodimer, the subunits of which were linked to each other via covalent disulfide bonds. Both female and male worms possessed monophenol oxidase and diphenol oxidase activities of TYR. The relative enzymatic activities were 0.165 $ min^{−1} $ $ mg^{−1} $ and 0.0805 $ min^{−1} $ $ mg^{−1} $, which were inhibited by a copper-chelating agent (allyl thiourea) and correlated with disruption of female egg production. Our results revealed that SjTYRs might play a significant role during eggshell formation. |
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Expression and characterization of two tyrosinases from the trematode Schistosoma japonicum |
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| score |
7.4020653 |