Document Detail

Affinity purification of endothia protease with a novel renin inhibitor SQ 32,970.
MedLine Citation:
PMID:  2658996     Owner:  NLM     Status:  MEDLINE    
A novel tripeptidic renin inhibitor is described, SQ 32,970, that will potently inhibit endothia protease. This inhibitor can be coupled to Sepharose and will allow the affinity-purification of endothia protease in one step to greater than 95% purity as measured by SDS PAGE. The purified endothia protease cleaves the Lys-Pro-Ala-Glu-Phe-Nph-Arg-Leu substrate at the Phe-Nph bond with a Kcat/Km of 7445 (s-1 mM-1) at pH 3.1 and 4057 (s-1 mM-1) at pH 6.0. Affinity purified endothia protease can be crystallized in the pH range in which it is enzymatically active and can be inhibited by renin inhibitors.
J A Norman; D Little; C A Free; T Dejneka; H Weber; D E Ryono
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  161     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  1989 May 
Date Detail:
Created Date:  1989-07-12     Completed Date:  1989-07-12     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1-7     Citation Subset:  IM    
Department of Pharmacology, Squibb Institute for Medical Research, Princeton, New Jersey.
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MeSH Terms
Ascomycota / analysis*
Aspartic Acid Endopeptidases*
Chromatography, High Pressure Liquid
Endopeptidases / isolation & purification*
Fungal Proteins / isolation & purification*
Molecular Weight
Oligopeptides / pharmacology*
Protease Inhibitors
Renin / antagonists & inhibitors*
Substrate Specificity
Reg. No./Substance:
0/Fungal Proteins; 0/Oligopeptides; 0/Protease Inhibitors; 122280-12-0/SQ 32970; EC 3.4.-/Endopeptidases; EC 3.4.23.-/Aspartic Acid Endopeptidases; EC 3.4.23.-/Endothia aspartic proteinase; EC

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