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A protease from the marine sponge Callyspongia schulzi
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| Zeitschriftentitel: | IUBMB Life |
|---|---|
| Personen und Körperschaften: | , , , , |
| In: | IUBMB Life, 42, 1997, 4, S. 789-797 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Mebs, Dietrich Benesch, Stefan König, Birgit Yamakawa, Yoshio Omori‐Satoh, Tamotsu Mebs, Dietrich Benesch, Stefan König, Birgit Yamakawa, Yoshio Omori‐Satoh, Tamotsu |
|---|---|
| author |
Mebs, Dietrich Benesch, Stefan König, Birgit Yamakawa, Yoshio Omori‐Satoh, Tamotsu |
| spellingShingle |
Mebs, Dietrich Benesch, Stefan König, Birgit Yamakawa, Yoshio Omori‐Satoh, Tamotsu IUBMB Life A protease from the marine sponge Callyspongia schulzi Cell Biology Clinical Biochemistry Genetics Molecular Biology Biochemistry |
| author_sort |
mebs, dietrich |
| spelling |
Mebs, Dietrich Benesch, Stefan König, Birgit Yamakawa, Yoshio Omori‐Satoh, Tamotsu 1521-6543 1521-6551 Wiley Cell Biology Clinical Biochemistry Genetics Molecular Biology Biochemistry http://dx.doi.org/10.1080/15216549700203221 <jats:title>Abstract</jats:title><jats:p>Aqueous extracts of 25 marine sponge species (from coral reefs of Papua New Guinea) were screened for proteolytic activity. Only one sponge, Callyspongia schulzi, showed remarkable activity. A protease hydrolyzing casein as well as the synthetic substrate α‐N‐benzoyl‐L‐arginine ethyl ester was isolated from the sponge extract by gel filtration, ion‐exchange and HPLC absorption chromatography. The enzyme was homogenous in SDS‐PAGE exhibiting an apparent molecular weight of 80 kDa. Its pH optimum was in the range of 9‐11, it was remarkably heat‐stable and was not inhibited by phenylmethane sulfonylfluoride, soybean trypsin inhibitor, aprotinin or α1‐antitrypsin, but by EDTA and 1,10‐phenanthroline suggesting properties of a metalloprotease. The protease hydrolyzed the oxidized insulin B‐chain between Arg22‐Gly23 and Lys29‐Ala30, similar to trypsin.</jats:p> A protease from the marine sponge Callyspongia schulzi IUBMB Life |
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Wiley, 1997 |
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Wiley, 1997 |
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| title |
A protease from the marine sponge Callyspongia schulzi |
| title_unstemmed |
A protease from the marine sponge Callyspongia schulzi |
| title_full |
A protease from the marine sponge Callyspongia schulzi |
| title_fullStr |
A protease from the marine sponge Callyspongia schulzi |
| title_full_unstemmed |
A protease from the marine sponge Callyspongia schulzi |
| title_short |
A protease from the marine sponge Callyspongia schulzi |
| title_sort |
a protease from the marine sponge callyspongia schulzi |
| topic |
Cell Biology Clinical Biochemistry Genetics Molecular Biology Biochemistry |
| url |
http://dx.doi.org/10.1080/15216549700203221 |
| publishDate |
1997 |
| physical |
789-797 |
| description |
<jats:title>Abstract</jats:title><jats:p>Aqueous extracts of 25 marine sponge species (from coral reefs of Papua New Guinea) were screened for proteolytic activity. Only one sponge, Callyspongia schulzi, showed remarkable activity. A protease hydrolyzing casein as well as the synthetic substrate α‐N‐benzoyl‐L‐arginine ethyl ester was isolated from the sponge extract by gel filtration, ion‐exchange and HPLC absorption chromatography. The enzyme was homogenous in SDS‐PAGE exhibiting an apparent molecular weight of 80 kDa. Its pH optimum was in the range of 9‐11, it was remarkably heat‐stable and was not inhibited by phenylmethane sulfonylfluoride, soybean trypsin inhibitor, aprotinin or α1‐antitrypsin, but by EDTA and 1,10‐phenanthroline suggesting properties of a metalloprotease. The protease hydrolyzed the oxidized insulin B‐chain between Arg22‐Gly23 and Lys29‐Ala30, similar to trypsin.</jats:p> |
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| author | Mebs, Dietrich, Benesch, Stefan, König, Birgit, Yamakawa, Yoshio, Omori‐Satoh, Tamotsu |
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| description | <jats:title>Abstract</jats:title><jats:p>Aqueous extracts of 25 marine sponge species (from coral reefs of Papua New Guinea) were screened for proteolytic activity. Only one sponge, Callyspongia schulzi, showed remarkable activity. A protease hydrolyzing casein as well as the synthetic substrate α‐N‐benzoyl‐L‐arginine ethyl ester was isolated from the sponge extract by gel filtration, ion‐exchange and HPLC absorption chromatography. The enzyme was homogenous in SDS‐PAGE exhibiting an apparent molecular weight of 80 kDa. Its pH optimum was in the range of 9‐11, it was remarkably heat‐stable and was not inhibited by phenylmethane sulfonylfluoride, soybean trypsin inhibitor, aprotinin or α1‐antitrypsin, but by EDTA and 1,10‐phenanthroline suggesting properties of a metalloprotease. The protease hydrolyzed the oxidized insulin B‐chain between Arg22‐Gly23 and Lys29‐Ala30, similar to trypsin.</jats:p> |
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| imprint | Wiley, 1997 |
| imprint_str_mv | Wiley, 1997 |
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| source_id | 49 |
| spelling | Mebs, Dietrich Benesch, Stefan König, Birgit Yamakawa, Yoshio Omori‐Satoh, Tamotsu 1521-6543 1521-6551 Wiley Cell Biology Clinical Biochemistry Genetics Molecular Biology Biochemistry http://dx.doi.org/10.1080/15216549700203221 <jats:title>Abstract</jats:title><jats:p>Aqueous extracts of 25 marine sponge species (from coral reefs of Papua New Guinea) were screened for proteolytic activity. Only one sponge, Callyspongia schulzi, showed remarkable activity. A protease hydrolyzing casein as well as the synthetic substrate α‐N‐benzoyl‐L‐arginine ethyl ester was isolated from the sponge extract by gel filtration, ion‐exchange and HPLC absorption chromatography. The enzyme was homogenous in SDS‐PAGE exhibiting an apparent molecular weight of 80 kDa. Its pH optimum was in the range of 9‐11, it was remarkably heat‐stable and was not inhibited by phenylmethane sulfonylfluoride, soybean trypsin inhibitor, aprotinin or α1‐antitrypsin, but by EDTA and 1,10‐phenanthroline suggesting properties of a metalloprotease. The protease hydrolyzed the oxidized insulin B‐chain between Arg22‐Gly23 and Lys29‐Ala30, similar to trypsin.</jats:p> A protease from the marine sponge Callyspongia schulzi IUBMB Life |
| spellingShingle | Mebs, Dietrich, Benesch, Stefan, König, Birgit, Yamakawa, Yoshio, Omori‐Satoh, Tamotsu, IUBMB Life, A protease from the marine sponge Callyspongia schulzi, Cell Biology, Clinical Biochemistry, Genetics, Molecular Biology, Biochemistry |
| title | A protease from the marine sponge Callyspongia schulzi |
| title_full | A protease from the marine sponge Callyspongia schulzi |
| title_fullStr | A protease from the marine sponge Callyspongia schulzi |
| title_full_unstemmed | A protease from the marine sponge Callyspongia schulzi |
| title_short | A protease from the marine sponge Callyspongia schulzi |
| title_sort | a protease from the marine sponge callyspongia schulzi |
| title_unstemmed | A protease from the marine sponge Callyspongia schulzi |
| topic | Cell Biology, Clinical Biochemistry, Genetics, Molecular Biology, Biochemistry |
| url | http://dx.doi.org/10.1080/15216549700203221 |