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Infect Immun ; 57(8): 2522-8, 1989 Aug.
Article in English | MEDLINE | ID: mdl-2744859

ABSTRACT

An enzyme from Bacteroides gingivalis SUNYAB A7A1-28 that hydrolyzes the synthetic peptide glycyl-L-proline 4-methoxy-beta-naphthylamide was purified 1,040-fold by urea extraction, gel filtration, ion-exchange chromatography, and fast protein liquid chromatography. The molecular weight of the enzyme was 80,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 75,000 as determined by gel filtration. The optimum pH for the hydrolysis of glycyl-L-proline 4-methoxy-beta-naphthylamide was 7.5 to 8.5. The enzyme activity was inhibited by the serine protease inhibitors diisopropyl fluorophosphate and phenylmethylsulfonyl fluoride by 82.5 and 78%, respectively. The activity was also inhibited by Hg2+ (55.6%) and Zn2+ (45%).


Subject(s)
Bacterial Proteins/isolation & purification , Bacteroides/enzymology , Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/isolation & purification , Collagen/metabolism , Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/antagonists & inhibitors , Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/metabolism , Mercury/pharmacology , Molecular Weight , Protease Inhibitors/pharmacology , Substrate Specificity , Zinc/pharmacology
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