Document Detail


Action of human lysosomal elastase on the oxidized B chain of insulin.
MedLine Citation:
PMID:  851414     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The specificity of action of the lysosomal elastase of human neutrophil leucocytes on the oxidized B chain of insulin is similar to that of pig pancreatic elastase, but is more directed towards valine than alanine as the residue contributing the carboxyl group of the cleaved bond. The most susceptible bonds are Val-12-Glu-13 and Val-18-Cys(O3H)-19. Other bonds hydrolysed are Ala-14-Leu-15, Ser-9-His-10 and Cys, (O3H3)-7-Gly-8. Tables listing amino acid composition, N-terminal residue, and yields of isolated peptides have been deposited as Supplementary Publication SUP 50 075 (8 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1977) 161, 1.
Authors:
A M Blow
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Biochemical journal     Volume:  161     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1977 Jan 
Date Detail:
Created Date:  1977-05-27     Completed Date:  1977-05-27     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  13-6     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / analysis
Humans
Insulin*
Lysosomes / enzymology*
Neutrophils / enzymology
Pancreatic Elastase*
Chemical
Reg. No./Substance:
0/Amino Acids; 11061-68-0/Insulin; EC 3.4.21.36/Pancreatic Elastase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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