Document Detail

Purification and properties of an extracellular protease from Myxococcus virescens.
MedLine Citation:
PMID:  22536     Owner:  NLM     Status:  MEDLINE    
An extracellular protease from Myxococcus virescens was purified by phosphate precipitation, gel exclusion, and ion-exchange chromatography. The enzyme appeared homogeneous upon disc electrophoresis. The molecular weight of the protease was estimated to be 26,000. The enzyme was rapidly inactivated by ethylenediaminetetraacetate, but the activity could be partially restored by divalent cations. Diisopropylphosphorofluoridate inhibited enzyme activity completely. Michaelis-Menten kinetics were obeyed with casein and hemoglobin as substrates. First-order kinetics were obtained with elastin as the substrate, provided trypsin was in excess. Petidolytic activity indicated that the peptide bonds hydrolyzed by the enzyme were mainly those involving amino acids with nonpolar side chains.
G Gnosspelius
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of bacteriology     Volume:  133     ISSN:  0021-9193     ISO Abbreviation:  J. Bacteriol.     Publication Date:  1978 Jan 
Date Detail:
Created Date:  1978-02-18     Completed Date:  1978-02-18     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  17-25     Citation Subset:  IM    
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MeSH Terms
Edetic Acid / pharmacology
Hydrogen-Ion Concentration
Isoflurophate / pharmacology
Molecular Weight
Myxococcales / enzymology*
Peptide Hydrolases / isolation & purification*,  metabolism
Protease Inhibitors
Reg. No./Substance:
0/Cations; 0/Protease Inhibitors; 55-91-4/Isoflurophate; 60-00-4/Edetic Acid; EC 3.4.-/Peptide Hydrolases

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

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