Ontology highlight
ABSTRACT:
SUBMITTER: Lin B
PROVIDER: S-EPMC174237 | biostudies-other | 1996 Aug
REPOSITORIES: biostudies-other
Lin B B Averett W F WF Novak J J Chatham W W WW Hollingshead S K SK Coligan J E JE Egan M L ML Pritchard D G DG
Infection and immunity 19960801 8
Group B streptococci were recently reported to possess a cell-associated collagenase. Although the enzyme hydrolyzed the synthetic collagen-like substrate N-(3-[2-furyl]acryloyl)-Leu-Gly-Pro-Ala, we found that neither the highly purified enzyme nor crude group B streptococcal cell lysate solubilized a film of reconstituted rat tail collagen, an activity regarded as obligatory for a true collagenase. We cloned and sequenced the gene for the enzyme (pepB). The deduced amino acid sequence showed 66 ...[more]