First serine protease inhibitor isolated from Rhinella schneideri poison
Background Toad secretions are a source of molecules with potential biotechnological application on a wide spectrum of diseases. Toads from the Rhinella family have two kinds of poisonous glands, namely granular and mucous glands. Rhinella schneideri toads produce granular secretions that comprise a...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Shibao, Priscila Y T [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Schlagwörter: |
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| Anmerkung: |
© Shibao et al. 2015 |
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| Übergeordnetes Werk: |
Enthalten in: The journal of venomous animals and toxins including tropical diseases - Botucatu : CEVAP, 1995, 21(2015), 1 vom: 13. Aug. |
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| Übergeordnetes Werk: |
volume:21 ; year:2015 ; number:1 ; day:13 ; month:08 |
| Links: |
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| DOI / URN: |
10.1186/s40409-015-0029-4 |
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| Katalog-ID: |
SPR036398950 |
|---|
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| 520 | |a Background Toad secretions are a source of molecules with potential biotechnological application on a wide spectrum of diseases. Toads from the Rhinella family have two kinds of poisonous glands, namely granular and mucous glands. Rhinella schneideri toads produce granular secretions that comprise a great number of molecules, including serine proteases inhibitors. Serine proteases, such as trypsin, chymotrypsin and elastase, are enzymes that have a serine amino acid into its catalytic site and can be found in a large number of vertebrate species and pathogenic microorganisms. Therefore, the present work aims to purify a serine protease inhibitor from Rhinella schneideri granular secretions. Findings This study presents the protocol used to purify a serine protease inhibitor from the Rhinella schneideri poison. The granular secretion was submitted to dialysis in order to separate the low molecular weight compounds, which were submitted to a reversed phase-fast protein liquid chromatography fractionation step in a C2C18 column. The major fractions were tested over trypsin, chymotrypsin and elastase through colorimetric assay. The inhibition tests were performed with the enzyme in absence (positive control) and presence of fractions, denatured enzyme (negative control) and the respective chromogenic substrate. Rs20 was the compound with the major inhibitory activity over chymotrypsin, inducing a delay in the formation of the chromogenic enzymatic product. The structure characterization of Rs20 was performed by high resolution electronspray ionization-mass spectrometry (HRESI-MS) and gas chromatography coupled with mass spectrometry (GC-MS). HRESI showed an intense signal suggesting the presence of bufadienolide with less than 10 ppm error. In addition, it was observed a low intense signal at m/z 399 that could be lithocholic acid, a biosynthetic precursor of bufadienolide. Finally, GC-MS analysis applying NIST library identification reinforced this hypothesis. Conclusions The current study have isolated and partially characterized the function and structure of the first bufadienolide with inhibitory action over chymotrypsin. | ||
| 650 | 4 | |a Bufadienolide |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Rhinella schneideri |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Serine protease inhibitor |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Anjolette, Fernando A P |4 aut | |
| 700 | 1 | |a Lopes, Norberto P. |4 aut | |
| 700 | 1 | |a Arantes, Eliane C. |4 aut | |
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10.1186/s40409-015-0029-4 doi (DE-627)SPR036398950 (SPR)s40409-015-0029-4-e DE-627 ger DE-627 rakwb eng Shibao, Priscila Y T verfasserin aut First serine protease inhibitor isolated from Rhinella schneideri poison 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Shibao et al. 2015 Background Toad secretions are a source of molecules with potential biotechnological application on a wide spectrum of diseases. Toads from the Rhinella family have two kinds of poisonous glands, namely granular and mucous glands. Rhinella schneideri toads produce granular secretions that comprise a great number of molecules, including serine proteases inhibitors. Serine proteases, such as trypsin, chymotrypsin and elastase, are enzymes that have a serine amino acid into its catalytic site and can be found in a large number of vertebrate species and pathogenic microorganisms. Therefore, the present work aims to purify a serine protease inhibitor from Rhinella schneideri granular secretions. Findings This study presents the protocol used to purify a serine protease inhibitor from the Rhinella schneideri poison. The granular secretion was submitted to dialysis in order to separate the low molecular weight compounds, which were submitted to a reversed phase-fast protein liquid chromatography fractionation step in a C2C18 column. The major fractions were tested over trypsin, chymotrypsin and elastase through colorimetric assay. The inhibition tests were performed with the enzyme in absence (positive control) and presence of fractions, denatured enzyme (negative control) and the respective chromogenic substrate. Rs20 was the compound with the major inhibitory activity over chymotrypsin, inducing a delay in the formation of the chromogenic enzymatic product. The structure characterization of Rs20 was performed by high resolution electronspray ionization-mass spectrometry (HRESI-MS) and gas chromatography coupled with mass spectrometry (GC-MS). HRESI showed an intense signal suggesting the presence of bufadienolide with less than 10 ppm error. In addition, it was observed a low intense signal at m/z 399 that could be lithocholic acid, a biosynthetic precursor of bufadienolide. Finally, GC-MS analysis applying NIST library identification reinforced this hypothesis. Conclusions The current study have isolated and partially characterized the function and structure of the first bufadienolide with inhibitory action over chymotrypsin. Bufadienolide (dpeaa)DE-He213 Rhinella schneideri (dpeaa)DE-He213 Serine protease inhibitor (dpeaa)DE-He213 Anjolette, Fernando A P aut Lopes, Norberto P. aut Arantes, Eliane C. aut Enthalten in The journal of venomous animals and toxins including tropical diseases Botucatu : CEVAP, 1995 21(2015), 1 vom: 13. Aug. (DE-627)324824459 (DE-600)2031021-3 1678-9199 nnns volume:21 year:2015 number:1 day:13 month:08 https://dx.doi.org/10.1186/s40409-015-0029-4 kostenfrei 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_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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2015 1 13 08 |
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10.1186/s40409-015-0029-4 doi (DE-627)SPR036398950 (SPR)s40409-015-0029-4-e DE-627 ger DE-627 rakwb eng Shibao, Priscila Y T verfasserin aut First serine protease inhibitor isolated from Rhinella schneideri poison 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Shibao et al. 2015 Background Toad secretions are a source of molecules with potential biotechnological application on a wide spectrum of diseases. Toads from the Rhinella family have two kinds of poisonous glands, namely granular and mucous glands. Rhinella schneideri toads produce granular secretions that comprise a great number of molecules, including serine proteases inhibitors. Serine proteases, such as trypsin, chymotrypsin and elastase, are enzymes that have a serine amino acid into its catalytic site and can be found in a large number of vertebrate species and pathogenic microorganisms. Therefore, the present work aims to purify a serine protease inhibitor from Rhinella schneideri granular secretions. Findings This study presents the protocol used to purify a serine protease inhibitor from the Rhinella schneideri poison. The granular secretion was submitted to dialysis in order to separate the low molecular weight compounds, which were submitted to a reversed phase-fast protein liquid chromatography fractionation step in a C2C18 column. The major fractions were tested over trypsin, chymotrypsin and elastase through colorimetric assay. The inhibition tests were performed with the enzyme in absence (positive control) and presence of fractions, denatured enzyme (negative control) and the respective chromogenic substrate. Rs20 was the compound with the major inhibitory activity over chymotrypsin, inducing a delay in the formation of the chromogenic enzymatic product. The structure characterization of Rs20 was performed by high resolution electronspray ionization-mass spectrometry (HRESI-MS) and gas chromatography coupled with mass spectrometry (GC-MS). HRESI showed an intense signal suggesting the presence of bufadienolide with less than 10 ppm error. In addition, it was observed a low intense signal at m/z 399 that could be lithocholic acid, a biosynthetic precursor of bufadienolide. Finally, GC-MS analysis applying NIST library identification reinforced this hypothesis. Conclusions The current study have isolated and partially characterized the function and structure of the first bufadienolide with inhibitory action over chymotrypsin. Bufadienolide (dpeaa)DE-He213 Rhinella schneideri (dpeaa)DE-He213 Serine protease inhibitor (dpeaa)DE-He213 Anjolette, Fernando A P aut Lopes, Norberto P. aut Arantes, Eliane C. aut Enthalten in The journal of venomous animals and toxins including tropical diseases Botucatu : CEVAP, 1995 21(2015), 1 vom: 13. Aug. (DE-627)324824459 (DE-600)2031021-3 1678-9199 nnns volume:21 year:2015 number:1 day:13 month:08 https://dx.doi.org/10.1186/s40409-015-0029-4 kostenfrei 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_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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2015 1 13 08 |
| allfields_unstemmed |
10.1186/s40409-015-0029-4 doi (DE-627)SPR036398950 (SPR)s40409-015-0029-4-e DE-627 ger DE-627 rakwb eng Shibao, Priscila Y T verfasserin aut First serine protease inhibitor isolated from Rhinella schneideri poison 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Shibao et al. 2015 Background Toad secretions are a source of molecules with potential biotechnological application on a wide spectrum of diseases. Toads from the Rhinella family have two kinds of poisonous glands, namely granular and mucous glands. Rhinella schneideri toads produce granular secretions that comprise a great number of molecules, including serine proteases inhibitors. Serine proteases, such as trypsin, chymotrypsin and elastase, are enzymes that have a serine amino acid into its catalytic site and can be found in a large number of vertebrate species and pathogenic microorganisms. Therefore, the present work aims to purify a serine protease inhibitor from Rhinella schneideri granular secretions. Findings This study presents the protocol used to purify a serine protease inhibitor from the Rhinella schneideri poison. The granular secretion was submitted to dialysis in order to separate the low molecular weight compounds, which were submitted to a reversed phase-fast protein liquid chromatography fractionation step in a C2C18 column. The major fractions were tested over trypsin, chymotrypsin and elastase through colorimetric assay. The inhibition tests were performed with the enzyme in absence (positive control) and presence of fractions, denatured enzyme (negative control) and the respective chromogenic substrate. Rs20 was the compound with the major inhibitory activity over chymotrypsin, inducing a delay in the formation of the chromogenic enzymatic product. The structure characterization of Rs20 was performed by high resolution electronspray ionization-mass spectrometry (HRESI-MS) and gas chromatography coupled with mass spectrometry (GC-MS). HRESI showed an intense signal suggesting the presence of bufadienolide with less than 10 ppm error. In addition, it was observed a low intense signal at m/z 399 that could be lithocholic acid, a biosynthetic precursor of bufadienolide. Finally, GC-MS analysis applying NIST library identification reinforced this hypothesis. Conclusions The current study have isolated and partially characterized the function and structure of the first bufadienolide with inhibitory action over chymotrypsin. Bufadienolide (dpeaa)DE-He213 Rhinella schneideri (dpeaa)DE-He213 Serine protease inhibitor (dpeaa)DE-He213 Anjolette, Fernando A P aut Lopes, Norberto P. aut Arantes, Eliane C. aut Enthalten in The journal of venomous animals and toxins including tropical diseases Botucatu : CEVAP, 1995 21(2015), 1 vom: 13. Aug. (DE-627)324824459 (DE-600)2031021-3 1678-9199 nnns volume:21 year:2015 number:1 day:13 month:08 https://dx.doi.org/10.1186/s40409-015-0029-4 kostenfrei 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_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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2015 1 13 08 |
| allfieldsGer |
10.1186/s40409-015-0029-4 doi (DE-627)SPR036398950 (SPR)s40409-015-0029-4-e DE-627 ger DE-627 rakwb eng Shibao, Priscila Y T verfasserin aut First serine protease inhibitor isolated from Rhinella schneideri poison 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Shibao et al. 2015 Background Toad secretions are a source of molecules with potential biotechnological application on a wide spectrum of diseases. Toads from the Rhinella family have two kinds of poisonous glands, namely granular and mucous glands. Rhinella schneideri toads produce granular secretions that comprise a great number of molecules, including serine proteases inhibitors. Serine proteases, such as trypsin, chymotrypsin and elastase, are enzymes that have a serine amino acid into its catalytic site and can be found in a large number of vertebrate species and pathogenic microorganisms. Therefore, the present work aims to purify a serine protease inhibitor from Rhinella schneideri granular secretions. Findings This study presents the protocol used to purify a serine protease inhibitor from the Rhinella schneideri poison. The granular secretion was submitted to dialysis in order to separate the low molecular weight compounds, which were submitted to a reversed phase-fast protein liquid chromatography fractionation step in a C2C18 column. The major fractions were tested over trypsin, chymotrypsin and elastase through colorimetric assay. The inhibition tests were performed with the enzyme in absence (positive control) and presence of fractions, denatured enzyme (negative control) and the respective chromogenic substrate. Rs20 was the compound with the major inhibitory activity over chymotrypsin, inducing a delay in the formation of the chromogenic enzymatic product. The structure characterization of Rs20 was performed by high resolution electronspray ionization-mass spectrometry (HRESI-MS) and gas chromatography coupled with mass spectrometry (GC-MS). HRESI showed an intense signal suggesting the presence of bufadienolide with less than 10 ppm error. In addition, it was observed a low intense signal at m/z 399 that could be lithocholic acid, a biosynthetic precursor of bufadienolide. Finally, GC-MS analysis applying NIST library identification reinforced this hypothesis. Conclusions The current study have isolated and partially characterized the function and structure of the first bufadienolide with inhibitory action over chymotrypsin. Bufadienolide (dpeaa)DE-He213 Rhinella schneideri (dpeaa)DE-He213 Serine protease inhibitor (dpeaa)DE-He213 Anjolette, Fernando A P aut Lopes, Norberto P. aut Arantes, Eliane C. aut Enthalten in The journal of venomous animals and toxins including tropical diseases Botucatu : CEVAP, 1995 21(2015), 1 vom: 13. Aug. (DE-627)324824459 (DE-600)2031021-3 1678-9199 nnns volume:21 year:2015 number:1 day:13 month:08 https://dx.doi.org/10.1186/s40409-015-0029-4 kostenfrei 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_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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2015 1 13 08 |
| allfieldsSound |
10.1186/s40409-015-0029-4 doi (DE-627)SPR036398950 (SPR)s40409-015-0029-4-e DE-627 ger DE-627 rakwb eng Shibao, Priscila Y T verfasserin aut First serine protease inhibitor isolated from Rhinella schneideri poison 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Shibao et al. 2015 Background Toad secretions are a source of molecules with potential biotechnological application on a wide spectrum of diseases. Toads from the Rhinella family have two kinds of poisonous glands, namely granular and mucous glands. Rhinella schneideri toads produce granular secretions that comprise a great number of molecules, including serine proteases inhibitors. Serine proteases, such as trypsin, chymotrypsin and elastase, are enzymes that have a serine amino acid into its catalytic site and can be found in a large number of vertebrate species and pathogenic microorganisms. Therefore, the present work aims to purify a serine protease inhibitor from Rhinella schneideri granular secretions. Findings This study presents the protocol used to purify a serine protease inhibitor from the Rhinella schneideri poison. The granular secretion was submitted to dialysis in order to separate the low molecular weight compounds, which were submitted to a reversed phase-fast protein liquid chromatography fractionation step in a C2C18 column. The major fractions were tested over trypsin, chymotrypsin and elastase through colorimetric assay. The inhibition tests were performed with the enzyme in absence (positive control) and presence of fractions, denatured enzyme (negative control) and the respective chromogenic substrate. Rs20 was the compound with the major inhibitory activity over chymotrypsin, inducing a delay in the formation of the chromogenic enzymatic product. The structure characterization of Rs20 was performed by high resolution electronspray ionization-mass spectrometry (HRESI-MS) and gas chromatography coupled with mass spectrometry (GC-MS). HRESI showed an intense signal suggesting the presence of bufadienolide with less than 10 ppm error. In addition, it was observed a low intense signal at m/z 399 that could be lithocholic acid, a biosynthetic precursor of bufadienolide. Finally, GC-MS analysis applying NIST library identification reinforced this hypothesis. Conclusions The current study have isolated and partially characterized the function and structure of the first bufadienolide with inhibitory action over chymotrypsin. Bufadienolide (dpeaa)DE-He213 Rhinella schneideri (dpeaa)DE-He213 Serine protease inhibitor (dpeaa)DE-He213 Anjolette, Fernando A P aut Lopes, Norberto P. aut Arantes, Eliane C. aut Enthalten in The journal of venomous animals and toxins including tropical diseases Botucatu : CEVAP, 1995 21(2015), 1 vom: 13. Aug. (DE-627)324824459 (DE-600)2031021-3 1678-9199 nnns volume:21 year:2015 number:1 day:13 month:08 https://dx.doi.org/10.1186/s40409-015-0029-4 kostenfrei 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_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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2015 1 13 08 |
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Shibao, Priscila Y T |
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Shibao, Priscila Y T misc Bufadienolide misc Rhinella schneideri misc Serine protease inhibitor First serine protease inhibitor isolated from Rhinella schneideri poison |
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First serine protease inhibitor isolated from Rhinella schneideri poison Bufadienolide (dpeaa)DE-He213 Rhinella schneideri (dpeaa)DE-He213 Serine protease inhibitor (dpeaa)DE-He213 |
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first serine protease inhibitor isolated from rhinella schneideri poison |
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First serine protease inhibitor isolated from Rhinella schneideri poison |
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Background Toad secretions are a source of molecules with potential biotechnological application on a wide spectrum of diseases. Toads from the Rhinella family have two kinds of poisonous glands, namely granular and mucous glands. Rhinella schneideri toads produce granular secretions that comprise a great number of molecules, including serine proteases inhibitors. Serine proteases, such as trypsin, chymotrypsin and elastase, are enzymes that have a serine amino acid into its catalytic site and can be found in a large number of vertebrate species and pathogenic microorganisms. Therefore, the present work aims to purify a serine protease inhibitor from Rhinella schneideri granular secretions. Findings This study presents the protocol used to purify a serine protease inhibitor from the Rhinella schneideri poison. The granular secretion was submitted to dialysis in order to separate the low molecular weight compounds, which were submitted to a reversed phase-fast protein liquid chromatography fractionation step in a C2C18 column. The major fractions were tested over trypsin, chymotrypsin and elastase through colorimetric assay. The inhibition tests were performed with the enzyme in absence (positive control) and presence of fractions, denatured enzyme (negative control) and the respective chromogenic substrate. Rs20 was the compound with the major inhibitory activity over chymotrypsin, inducing a delay in the formation of the chromogenic enzymatic product. The structure characterization of Rs20 was performed by high resolution electronspray ionization-mass spectrometry (HRESI-MS) and gas chromatography coupled with mass spectrometry (GC-MS). HRESI showed an intense signal suggesting the presence of bufadienolide with less than 10 ppm error. In addition, it was observed a low intense signal at m/z 399 that could be lithocholic acid, a biosynthetic precursor of bufadienolide. Finally, GC-MS analysis applying NIST library identification reinforced this hypothesis. Conclusions The current study have isolated and partially characterized the function and structure of the first bufadienolide with inhibitory action over chymotrypsin. © Shibao et al. 2015 |
| abstractGer |
Background Toad secretions are a source of molecules with potential biotechnological application on a wide spectrum of diseases. Toads from the Rhinella family have two kinds of poisonous glands, namely granular and mucous glands. Rhinella schneideri toads produce granular secretions that comprise a great number of molecules, including serine proteases inhibitors. Serine proteases, such as trypsin, chymotrypsin and elastase, are enzymes that have a serine amino acid into its catalytic site and can be found in a large number of vertebrate species and pathogenic microorganisms. Therefore, the present work aims to purify a serine protease inhibitor from Rhinella schneideri granular secretions. Findings This study presents the protocol used to purify a serine protease inhibitor from the Rhinella schneideri poison. The granular secretion was submitted to dialysis in order to separate the low molecular weight compounds, which were submitted to a reversed phase-fast protein liquid chromatography fractionation step in a C2C18 column. The major fractions were tested over trypsin, chymotrypsin and elastase through colorimetric assay. The inhibition tests were performed with the enzyme in absence (positive control) and presence of fractions, denatured enzyme (negative control) and the respective chromogenic substrate. Rs20 was the compound with the major inhibitory activity over chymotrypsin, inducing a delay in the formation of the chromogenic enzymatic product. The structure characterization of Rs20 was performed by high resolution electronspray ionization-mass spectrometry (HRESI-MS) and gas chromatography coupled with mass spectrometry (GC-MS). HRESI showed an intense signal suggesting the presence of bufadienolide with less than 10 ppm error. In addition, it was observed a low intense signal at m/z 399 that could be lithocholic acid, a biosynthetic precursor of bufadienolide. Finally, GC-MS analysis applying NIST library identification reinforced this hypothesis. Conclusions The current study have isolated and partially characterized the function and structure of the first bufadienolide with inhibitory action over chymotrypsin. © Shibao et al. 2015 |
| abstract_unstemmed |
Background Toad secretions are a source of molecules with potential biotechnological application on a wide spectrum of diseases. Toads from the Rhinella family have two kinds of poisonous glands, namely granular and mucous glands. Rhinella schneideri toads produce granular secretions that comprise a great number of molecules, including serine proteases inhibitors. Serine proteases, such as trypsin, chymotrypsin and elastase, are enzymes that have a serine amino acid into its catalytic site and can be found in a large number of vertebrate species and pathogenic microorganisms. Therefore, the present work aims to purify a serine protease inhibitor from Rhinella schneideri granular secretions. Findings This study presents the protocol used to purify a serine protease inhibitor from the Rhinella schneideri poison. The granular secretion was submitted to dialysis in order to separate the low molecular weight compounds, which were submitted to a reversed phase-fast protein liquid chromatography fractionation step in a C2C18 column. The major fractions were tested over trypsin, chymotrypsin and elastase through colorimetric assay. The inhibition tests were performed with the enzyme in absence (positive control) and presence of fractions, denatured enzyme (negative control) and the respective chromogenic substrate. Rs20 was the compound with the major inhibitory activity over chymotrypsin, inducing a delay in the formation of the chromogenic enzymatic product. The structure characterization of Rs20 was performed by high resolution electronspray ionization-mass spectrometry (HRESI-MS) and gas chromatography coupled with mass spectrometry (GC-MS). HRESI showed an intense signal suggesting the presence of bufadienolide with less than 10 ppm error. In addition, it was observed a low intense signal at m/z 399 that could be lithocholic acid, a biosynthetic precursor of bufadienolide. Finally, GC-MS analysis applying NIST library identification reinforced this hypothesis. Conclusions The current study have isolated and partially characterized the function and structure of the first bufadienolide with inhibitory action over chymotrypsin. © Shibao et al. 2015 |
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Toads from the Rhinella family have two kinds of poisonous glands, namely granular and mucous glands. Rhinella schneideri toads produce granular secretions that comprise a great number of molecules, including serine proteases inhibitors. Serine proteases, such as trypsin, chymotrypsin and elastase, are enzymes that have a serine amino acid into its catalytic site and can be found in a large number of vertebrate species and pathogenic microorganisms. Therefore, the present work aims to purify a serine protease inhibitor from Rhinella schneideri granular secretions. Findings This study presents the protocol used to purify a serine protease inhibitor from the Rhinella schneideri poison. The granular secretion was submitted to dialysis in order to separate the low molecular weight compounds, which were submitted to a reversed phase-fast protein liquid chromatography fractionation step in a C2C18 column. The major fractions were tested over trypsin, chymotrypsin and elastase through colorimetric assay. The inhibition tests were performed with the enzyme in absence (positive control) and presence of fractions, denatured enzyme (negative control) and the respective chromogenic substrate. Rs20 was the compound with the major inhibitory activity over chymotrypsin, inducing a delay in the formation of the chromogenic enzymatic product. The structure characterization of Rs20 was performed by high resolution electronspray ionization-mass spectrometry (HRESI-MS) and gas chromatography coupled with mass spectrometry (GC-MS). HRESI showed an intense signal suggesting the presence of bufadienolide with less than 10 ppm error. In addition, it was observed a low intense signal at m/z 399 that could be lithocholic acid, a biosynthetic precursor of bufadienolide. Finally, GC-MS analysis applying NIST library identification reinforced this hypothesis. Conclusions The current study have isolated and partially characterized the function and structure of the first bufadienolide with inhibitory action over chymotrypsin.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Bufadienolide</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Rhinella schneideri</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Serine protease inhibitor</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Anjolette, Fernando A P</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lopes, Norberto P.</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Arantes, Eliane C.</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">The journal of venomous animals and toxins including tropical diseases</subfield><subfield code="d">Botucatu : CEVAP, 1995</subfield><subfield code="g">21(2015), 1 vom: 13. 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