Role of the chymotrypsin-like membrane-associated proteinase from Treponema denticola ATCC 35405 in inactivation of bioactive peptides.

The ability of washed whole cells of Treponema denticola ATCC 35405 to hydrolyze (inactivate) substance P, bradykinin, and angiotensin I was studied. Substance P was attacked primarily at the Phe-8-Gly-9 bond by a chymotrypsin-like proteinase (CTLP), at Pro-4-Gln-5 by an endo-acting prolyl oligopept...

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Vydáno v:	Infect Immun
Hlavní autoři:	Mäkinen, P L, Mäkinen, K K, Syed, S A
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	American Society for Microbiology (ASM) 1995
Témata:	Research Article
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC173495/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7543886/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/iai.63.9.3567-3575.1995
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