Studies on Fin Whale Pancreatic Proteases: III. Properties of Purified Fin Whale Anionic Chymotrypsin
Some physical and enzymatic properties were studied on the purified fin whale anionic chymotrypsin which was homogeneous by polyacrylamide gel electrophoresis and ultracentrifugal analysis. The molecular weight was approximately 17, 000 ( S 20 , w = 1.62) by the Archibald procedure, and the enzyme w...
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1970
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fthighwire:oai:open-archive.highwire.org:jbiochem:68/1/1 2023-05-15T16:13:15+02:00 Studies on Fin Whale Pancreatic Proteases: III. Properties of Purified Fin Whale Anionic Chymotrypsin MATSUOKA, Atsushi KOIDE and Yoshitaka 1970-07-01 00:00:00.0 text/html http://jb.oxfordjournals.org/cgi/content/short/68/1/1 en eng Oxford University Press http://jb.oxfordjournals.org/cgi/content/short/68/1/1 Copyright (C) 1970, Japanese Biochemical Society Articles TEXT 1970 fthighwire 2013-05-28T00:35:43Z Some physical and enzymatic properties were studied on the purified fin whale anionic chymotrypsin which was homogeneous by polyacrylamide gel electrophoresis and ultracentrifugal analysis. The molecular weight was approximately 17, 000 ( S 20 , w = 1.62) by the Archibald procedure, and the enzyme was found to be composed of approximately 126 amino acid residues. The isoelectric point was 5.2 (μ=0.1). The optimum pH for caseinolytic and N-acetyl-L-tyrosine ethyl ester hydrolyzing activities were about pH 8.0 and pH 7.5, respectively. The fin whale anionic enzyme was inhibited by DFP, like bovine pancreatic proteases, but not inhibited by N-tosyl-phenylalanine chloromethyl ketone. As far as the effects of bivalent cations, and natural trypsin inhibitors are concerned, no significant differences were found between fin whale and bovine anionic chymotrypsins. The substrate specificity was similar to that of bovine chymotrypsins B and α [EC 3.4.4.6 and 5]. Text Fin whale HighWire Press (Stanford University) Archibald ENVELOPE(-56.692,-56.692,-63.209,-63.209) |
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HighWire Press (Stanford University) |
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English |
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Articles |
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Articles MATSUOKA, Atsushi KOIDE and Yoshitaka Studies on Fin Whale Pancreatic Proteases: III. Properties of Purified Fin Whale Anionic Chymotrypsin |
topic_facet |
Articles |
description |
Some physical and enzymatic properties were studied on the purified fin whale anionic chymotrypsin which was homogeneous by polyacrylamide gel electrophoresis and ultracentrifugal analysis. The molecular weight was approximately 17, 000 ( S 20 , w = 1.62) by the Archibald procedure, and the enzyme was found to be composed of approximately 126 amino acid residues. The isoelectric point was 5.2 (μ=0.1). The optimum pH for caseinolytic and N-acetyl-L-tyrosine ethyl ester hydrolyzing activities were about pH 8.0 and pH 7.5, respectively. The fin whale anionic enzyme was inhibited by DFP, like bovine pancreatic proteases, but not inhibited by N-tosyl-phenylalanine chloromethyl ketone. As far as the effects of bivalent cations, and natural trypsin inhibitors are concerned, no significant differences were found between fin whale and bovine anionic chymotrypsins. The substrate specificity was similar to that of bovine chymotrypsins B and α [EC 3.4.4.6 and 5]. |
format |
Text |
author |
MATSUOKA, Atsushi KOIDE and Yoshitaka |
author_facet |
MATSUOKA, Atsushi KOIDE and Yoshitaka |
author_sort |
MATSUOKA, Atsushi KOIDE and Yoshitaka |
title |
Studies on Fin Whale Pancreatic Proteases: III. Properties of Purified Fin Whale Anionic Chymotrypsin |
title_short |
Studies on Fin Whale Pancreatic Proteases: III. Properties of Purified Fin Whale Anionic Chymotrypsin |
title_full |
Studies on Fin Whale Pancreatic Proteases: III. Properties of Purified Fin Whale Anionic Chymotrypsin |
title_fullStr |
Studies on Fin Whale Pancreatic Proteases: III. Properties of Purified Fin Whale Anionic Chymotrypsin |
title_full_unstemmed |
Studies on Fin Whale Pancreatic Proteases: III. Properties of Purified Fin Whale Anionic Chymotrypsin |
title_sort |
studies on fin whale pancreatic proteases: iii. properties of purified fin whale anionic chymotrypsin |
publisher |
Oxford University Press |
publishDate |
1970 |
url |
http://jb.oxfordjournals.org/cgi/content/short/68/1/1 |
long_lat |
ENVELOPE(-56.692,-56.692,-63.209,-63.209) |
geographic |
Archibald |
geographic_facet |
Archibald |
genre |
Fin whale |
genre_facet |
Fin whale |
op_relation |
http://jb.oxfordjournals.org/cgi/content/short/68/1/1 |
op_rights |
Copyright (C) 1970, Japanese Biochemical Society |
_version_ |
1765998894785757184 |