Gastric proteases of the Greenland cod Gadus ogac . I. Isolation and kinetic properties
The zymogens of three gastric proteases of the Greenland cod (Gadus ogac) were isolated by exclusion chromatography and chromatofocusing. The cod zymogens were activated more rapidly at lower temperatures than porcine pepsinogen and, after activation, were further purified by exclusion chromatograph...
Published in: | Biochemistry and Cell Biology |
---|---|
Main Authors: | , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Canadian Science Publishing
1986
|
Subjects: | |
Online Access: | http://dx.doi.org/10.1139/o86-030 http://www.nrcresearchpress.com/doi/pdf/10.1139/o86-030 |
id |
crcansciencepubl:10.1139/o86-030 |
---|---|
record_format |
openpolar |
spelling |
crcansciencepubl:10.1139/o86-030 2024-04-28T08:19:36+00:00 Gastric proteases of the Greenland cod Gadus ogac . I. Isolation and kinetic properties Squires, E. James Haard, N. F. Feltham, L. A. W. 1986 http://dx.doi.org/10.1139/o86-030 http://www.nrcresearchpress.com/doi/pdf/10.1139/o86-030 en eng Canadian Science Publishing http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining Biochemistry and Cell Biology volume 64, issue 3, page 205-214 ISSN 0829-8211 1208-6002 Cell Biology Molecular Biology Biochemistry journal-article 1986 crcansciencepubl https://doi.org/10.1139/o86-030 2024-04-09T06:56:31Z The zymogens of three gastric proteases of the Greenland cod (Gadus ogac) were isolated by exclusion chromatography and chromatofocusing. The cod zymogens were activated more rapidly at lower temperatures than porcine pepsinogen and, after activation, were further purified by exclusion chromatography. The cod proteases had more alkaline pH optima and were active over a wider range of pH than porcine pepsin. The specific activity of porcine pepsin on protein substrates was greater than that of the individual cod proteases. However, the cod proteases had cumulative activity on protein substrates that was greater than the sum of their individual activities. Cod protease I was active on pepsin-specific substrates, and cod proteases 2 and 3 were active as gastricsin-specific substrates. All three cod proteases had greater milk-clotting activity and hydrolysed hemoglobin to a greater extent than porcine pepsin. The V max and K m,app of the cod proteases were dependent upon the substrate, and V max /K m,app values of the cod proteases were generally lower than porcine pepsin. It is suggested that the cod proteases together exhibit broad substrate specificity and maintain activity over a wide range of conditions to enhance protein digestion in the cod stomach. Article in Journal/Newspaper Gadus ogac Greenland Greenland cod Canadian Science Publishing Biochemistry and Cell Biology 64 3 205 214 |
institution |
Open Polar |
collection |
Canadian Science Publishing |
op_collection_id |
crcansciencepubl |
language |
English |
topic |
Cell Biology Molecular Biology Biochemistry |
spellingShingle |
Cell Biology Molecular Biology Biochemistry Squires, E. James Haard, N. F. Feltham, L. A. W. Gastric proteases of the Greenland cod Gadus ogac . I. Isolation and kinetic properties |
topic_facet |
Cell Biology Molecular Biology Biochemistry |
description |
The zymogens of three gastric proteases of the Greenland cod (Gadus ogac) were isolated by exclusion chromatography and chromatofocusing. The cod zymogens were activated more rapidly at lower temperatures than porcine pepsinogen and, after activation, were further purified by exclusion chromatography. The cod proteases had more alkaline pH optima and were active over a wider range of pH than porcine pepsin. The specific activity of porcine pepsin on protein substrates was greater than that of the individual cod proteases. However, the cod proteases had cumulative activity on protein substrates that was greater than the sum of their individual activities. Cod protease I was active on pepsin-specific substrates, and cod proteases 2 and 3 were active as gastricsin-specific substrates. All three cod proteases had greater milk-clotting activity and hydrolysed hemoglobin to a greater extent than porcine pepsin. The V max and K m,app of the cod proteases were dependent upon the substrate, and V max /K m,app values of the cod proteases were generally lower than porcine pepsin. It is suggested that the cod proteases together exhibit broad substrate specificity and maintain activity over a wide range of conditions to enhance protein digestion in the cod stomach. |
format |
Article in Journal/Newspaper |
author |
Squires, E. James Haard, N. F. Feltham, L. A. W. |
author_facet |
Squires, E. James Haard, N. F. Feltham, L. A. W. |
author_sort |
Squires, E. James |
title |
Gastric proteases of the Greenland cod Gadus ogac . I. Isolation and kinetic properties |
title_short |
Gastric proteases of the Greenland cod Gadus ogac . I. Isolation and kinetic properties |
title_full |
Gastric proteases of the Greenland cod Gadus ogac . I. Isolation and kinetic properties |
title_fullStr |
Gastric proteases of the Greenland cod Gadus ogac . I. Isolation and kinetic properties |
title_full_unstemmed |
Gastric proteases of the Greenland cod Gadus ogac . I. Isolation and kinetic properties |
title_sort |
gastric proteases of the greenland cod gadus ogac . i. isolation and kinetic properties |
publisher |
Canadian Science Publishing |
publishDate |
1986 |
url |
http://dx.doi.org/10.1139/o86-030 http://www.nrcresearchpress.com/doi/pdf/10.1139/o86-030 |
genre |
Gadus ogac Greenland Greenland cod |
genre_facet |
Gadus ogac Greenland Greenland cod |
op_source |
Biochemistry and Cell Biology volume 64, issue 3, page 205-214 ISSN 0829-8211 1208-6002 |
op_rights |
http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining |
op_doi |
https://doi.org/10.1139/o86-030 |
container_title |
Biochemistry and Cell Biology |
container_volume |
64 |
container_issue |
3 |
container_start_page |
205 |
op_container_end_page |
214 |
_version_ |
1797583020445663232 |