Glycylprolyl Dipeptidylaminopeptidase from Bacteroides gingivalis
- 1 February 1985
- journal article
- research article
- Published by SAGE Publications in Journal of Dental Research
- Vol. 64 (2) , 106-111
- https://doi.org/10.1177/00220345850640020201
Abstract
Dipeptidyl aminopeptidase activity was found in the culture medium of Bacteroides gingivalis 381. The enzyme, hydrolyzing glycylprolyl-4-methylcoumaryl-7-amide, was purified 750-fold from culture medium by ammonium sulfate precipitation, Sephadex G-200 gel filtration, and DEAE Bio Gel A column chromatography. The molecular weight, determined by gel filtration, was approximately 160,000. The isoelectric point of the enzyme, estimated by isoelectric focusing using polyacrylamide disk gel electrophoresis, was about pH 6.2. The optimum pH of the enzyme was about 8.0, and the Km value was 0.05 mM. The enzyme activity was strongly inhibited by phenylmethylsulfonylfluoride and diisopropylfluorophosphate. The purified enzyme specifically cleaved glycylprolyl dipeptide from partially digested type I collagen.This publication has 28 references indexed in Scilit:
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