Purification and characterization of trypsin from the poikilotherm Gadus morhua
A serine protease shown to be trypsin was purified from the pyloric caeca of Atlantic cod ( Gadus morhua ), and resolved into three differently charged species by chromatofocusing (pI 6.6, 6.2 and 5.5). All three trypsins had similar molecular mass of 24.2 kDa. N‐terminal amino acid sequence analysi...
Published in: | European Journal of Biochemistry |
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crwiley:10.1111/j.1432-1033.1989.tb14618.x 2024-06-02T08:03:08+00:00 Purification and characterization of trypsin from the poikilotherm Gadus morhua ÁGEIRSSON, Bjarni FOX, Jay W. BJARNASON, Jón B. 1989 http://dx.doi.org/10.1111/j.1432-1033.1989.tb14618.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1989.tb14618.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1989.tb14618.x en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor European Journal of Biochemistry volume 180, issue 1, page 85-94 ISSN 0014-2956 1432-1033 journal-article 1989 crwiley https://doi.org/10.1111/j.1432-1033.1989.tb14618.x 2024-05-03T11:11:17Z A serine protease shown to be trypsin was purified from the pyloric caeca of Atlantic cod ( Gadus morhua ), and resolved into three differently charged species by chromatofocusing (pI 6.6, 6.2 and 5.5). All three trypsins had similar molecular mass of 24.2 kDa. N‐terminal amino acid sequence analysis of cod trypsin showed considerable similarity with other known trypsins, particularily with dogfish and some mammalian trypsins. The apparent K m values determined at 25°C for the predominant form of Atlantic cod trypsin towards p ‐tosyl‐L‐arginine methyl ester and N ‐benzoyl‐L‐arginine P ‐nitroanilide were 29 μM and 77 μM respectively, which are notably lower values than those determined for bovine trypsin (46 μM and 650 μM respectively). The difference was particularly striking when the amidase activity of the enzymes was compared. Furthermore, the K cat values determined for the Atlantic cold trypsins were consistently higher than the values determined for bovine trypsin. The higher catalytic efficiency ( K cat / K m ) of Atlantic cod trypsin as compared to bovine trypsin may reflect an evolutionary adaptation of the poikilothermic species to low environmental temperatures. Article in Journal/Newspaper atlantic cod Gadus morhua Wiley Online Library European Journal of Biochemistry 180 1 85 94 |
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Open Polar |
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Wiley Online Library |
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crwiley |
language |
English |
description |
A serine protease shown to be trypsin was purified from the pyloric caeca of Atlantic cod ( Gadus morhua ), and resolved into three differently charged species by chromatofocusing (pI 6.6, 6.2 and 5.5). All three trypsins had similar molecular mass of 24.2 kDa. N‐terminal amino acid sequence analysis of cod trypsin showed considerable similarity with other known trypsins, particularily with dogfish and some mammalian trypsins. The apparent K m values determined at 25°C for the predominant form of Atlantic cod trypsin towards p ‐tosyl‐L‐arginine methyl ester and N ‐benzoyl‐L‐arginine P ‐nitroanilide were 29 μM and 77 μM respectively, which are notably lower values than those determined for bovine trypsin (46 μM and 650 μM respectively). The difference was particularly striking when the amidase activity of the enzymes was compared. Furthermore, the K cat values determined for the Atlantic cold trypsins were consistently higher than the values determined for bovine trypsin. The higher catalytic efficiency ( K cat / K m ) of Atlantic cod trypsin as compared to bovine trypsin may reflect an evolutionary adaptation of the poikilothermic species to low environmental temperatures. |
format |
Article in Journal/Newspaper |
author |
ÁGEIRSSON, Bjarni FOX, Jay W. BJARNASON, Jón B. |
spellingShingle |
ÁGEIRSSON, Bjarni FOX, Jay W. BJARNASON, Jón B. Purification and characterization of trypsin from the poikilotherm Gadus morhua |
author_facet |
ÁGEIRSSON, Bjarni FOX, Jay W. BJARNASON, Jón B. |
author_sort |
ÁGEIRSSON, Bjarni |
title |
Purification and characterization of trypsin from the poikilotherm Gadus morhua |
title_short |
Purification and characterization of trypsin from the poikilotherm Gadus morhua |
title_full |
Purification and characterization of trypsin from the poikilotherm Gadus morhua |
title_fullStr |
Purification and characterization of trypsin from the poikilotherm Gadus morhua |
title_full_unstemmed |
Purification and characterization of trypsin from the poikilotherm Gadus morhua |
title_sort |
purification and characterization of trypsin from the poikilotherm gadus morhua |
publisher |
Wiley |
publishDate |
1989 |
url |
http://dx.doi.org/10.1111/j.1432-1033.1989.tb14618.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1989.tb14618.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1989.tb14618.x |
genre |
atlantic cod Gadus morhua |
genre_facet |
atlantic cod Gadus morhua |
op_source |
European Journal of Biochemistry volume 180, issue 1, page 85-94 ISSN 0014-2956 1432-1033 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1111/j.1432-1033.1989.tb14618.x |
container_title |
European Journal of Biochemistry |
container_volume |
180 |
container_issue |
1 |
container_start_page |
85 |
op_container_end_page |
94 |
_version_ |
1800747596640157696 |