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Purification and characterization of a multicatalytic proteinase from Atlantic salmon (Salmo salar) muscle.

Authors
  • Stoknes, I
  • Rustad, T
Type
Published Article
Journal
Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology
Publisher
Elsevier
Publication Date
Aug 01, 1995
Volume
111
Issue
4
Pages
587–596
Identifiers
PMID: 8574923
Source
Medline
License
Unknown

Abstract

A high molecular mass alkaline proteinase was purified by DEAE-Sepharose and Mono Q chromatography. The mol. wt was estimated to be about 600,000. Under denaturing conditions, the enzyme dissociated into a cluster of subunits with mol. wt ranging from 25,000 to 30,000. The isoelectric point of the enzyme was about pH 7.3. The proteinase was able to hydrolyse N-terminal-blocked 4-methyl-7-coumarylamide substrates for either trypsin- or chymotrypsin-like activity. It was also able to hydrolyse haemoglobin and myosin at temperatures of about 60 degrees C. The activities responded to pH and some chemicals in different ways. The trypsin-like activity was clearly inhibited by several serine protease inhibitors. These results suggest that the enzyme is multicatalytic, having at least two different active sites.

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