Gastric proteases of the Greenland cod Gadus ogac. II. Structural properties
Three gastric proteases were isolated from the stomach mucosa of the Greenland cod (Gadus ogac). The cod proteases were all less stable to heating and protease 1 retained less activity at 5 °C when the pH was greater than 5 in comparison with porcine pepsin. The activities of cod proteases 1 and 2,...
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Canadian Science Publishing
1986
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crcansciencepubl:10.1139/o86-031 2024-09-15T18:07:23+00:00 Gastric proteases of the Greenland cod Gadus ogac. II. Structural properties Squires, E. James Haard, N. F. Feltham, L. A. W. 1986 http://dx.doi.org/10.1139/o86-031 http://www.nrcresearchpress.com/doi/pdf/10.1139/o86-031 en eng Canadian Science Publishing http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining Biochemistry and Cell Biology volume 64, issue 3, page 215-222 ISSN 0829-8211 1208-6002 journal-article 1986 crcansciencepubl https://doi.org/10.1139/o86-031 2024-07-11T04:12:02Z Three gastric proteases were isolated from the stomach mucosa of the Greenland cod (Gadus ogac). The cod proteases were all less stable to heating and protease 1 retained less activity at 5 °C when the pH was greater than 5 in comparison with porcine pepsin. The activities of cod proteases 1 and 2, with hemoglobin as the substrate, were doubled in the presence of 25 mM NaCl, while cod protease 3 and porcine pepsin were not stimulated by the salt. The cod proteases did not cross-react with antibodies raised against porcine pepsin. However, some cross-reactivity was noted with antibodies raised against proteases from psychrotrophic pseudomonads. The molecular weights of all the cod proteases were in the range of 36 000–38 000. The amino acid compositions of the cod proteases as compared by the Metzger difference index differed from the mammalian gastric proteases by about the same extent that pepsin, gastricsin, and chymosin differ from each other. Of the cod enzymes, protease 1 differed from mammalian gastric proteases, while cod proteases 3 was more like chymosin with respect to amino acid composition. Cod protease 1 had the lowest hydrophobicity index and chymosin had the highest. The hydrophobicity indices of cod proteases 2 and 3 were intermediate between that of porcine pepsin and bovine chymosin. It is suggested that the Greenland cod proteases represent less differentiated forms of gastric proteases than the mammalian pepsins, gastricsins, and chymosins. Article in Journal/Newspaper Gadus ogac Greenland Greenland cod Canadian Science Publishing Biochemistry and Cell Biology 64 3 215 222 |
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Canadian Science Publishing |
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English |
description |
Three gastric proteases were isolated from the stomach mucosa of the Greenland cod (Gadus ogac). The cod proteases were all less stable to heating and protease 1 retained less activity at 5 °C when the pH was greater than 5 in comparison with porcine pepsin. The activities of cod proteases 1 and 2, with hemoglobin as the substrate, were doubled in the presence of 25 mM NaCl, while cod protease 3 and porcine pepsin were not stimulated by the salt. The cod proteases did not cross-react with antibodies raised against porcine pepsin. However, some cross-reactivity was noted with antibodies raised against proteases from psychrotrophic pseudomonads. The molecular weights of all the cod proteases were in the range of 36 000–38 000. The amino acid compositions of the cod proteases as compared by the Metzger difference index differed from the mammalian gastric proteases by about the same extent that pepsin, gastricsin, and chymosin differ from each other. Of the cod enzymes, protease 1 differed from mammalian gastric proteases, while cod proteases 3 was more like chymosin with respect to amino acid composition. Cod protease 1 had the lowest hydrophobicity index and chymosin had the highest. The hydrophobicity indices of cod proteases 2 and 3 were intermediate between that of porcine pepsin and bovine chymosin. It is suggested that the Greenland cod proteases represent less differentiated forms of gastric proteases than the mammalian pepsins, gastricsins, and chymosins. |
format |
Article in Journal/Newspaper |
author |
Squires, E. James Haard, N. F. Feltham, L. A. W. |
spellingShingle |
Squires, E. James Haard, N. F. Feltham, L. A. W. Gastric proteases of the Greenland cod Gadus ogac. II. Structural properties |
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. II. Structural properties |
title_short |
Gastric proteases of the Greenland cod Gadus ogac. II. Structural properties |
title_full |
Gastric proteases of the Greenland cod Gadus ogac. II. Structural properties |
title_fullStr |
Gastric proteases of the Greenland cod Gadus ogac. II. Structural properties |
title_full_unstemmed |
Gastric proteases of the Greenland cod Gadus ogac. II. Structural properties |
title_sort |
gastric proteases of the greenland cod gadus ogac. ii. structural properties |
publisher |
Canadian Science Publishing |
publishDate |
1986 |
url |
http://dx.doi.org/10.1139/o86-031 http://www.nrcresearchpress.com/doi/pdf/10.1139/o86-031 |
genre |
Gadus ogac Greenland Greenland cod |
genre_facet |
Gadus ogac Greenland Greenland cod |
op_source |
Biochemistry and Cell Biology volume 64, issue 3, page 215-222 ISSN 0829-8211 1208-6002 |
op_rights |
http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining |
op_doi |
https://doi.org/10.1139/o86-031 |
container_title |
Biochemistry and Cell Biology |
container_volume |
64 |
container_issue |
3 |
container_start_page |
215 |
op_container_end_page |
222 |
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1810444766604689408 |