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Proteolytic profile of <em>Treponema vincentii</em> ATCC 35580 with special reference to collagenolytic and arginine aminopeptidase activity.
- Source :
- Oral Microbiology & Immunology; Sep1988, Vol. 3 Issue 3, p121-128, 8p
- Publication Year :
- 1988
-
Abstract
- The proteolytic profile of <em>Treponema vincentii</em> ATCC 35580 was studied using PZ- PLGPA (phenylazobenzyloxycarbonyl-L-prolyl-L-leucylglycyl-L-prolyl-D-arginine; a substrate of bacterial collagenases) and amino acid 2-naphthylamides (2NA) as substrates. The cell extracts showed high activity toward PZ-PLGPA, <em>N</em>α-L-arginyl-2NA and <em>N</em>γ-L-glutamyl-2NA. Gel permeation chromatography revealed 2 major endopeptidases (I and II) hydrolyzing PZ-PLGPA, the molecular weights of which were 75,000 and 23,000, respectively. Enzyme I was stable enough for subsequent fast protein liquid chromatography on an anion exchange column. The enzyme had a broad pH optimum of 6.5 to 7.5 with PZ-PLGPA as substrate, hydrolyzed gelatin and was moderately inhibited by metal chelators, but was very sensitive to <em>p</em>-chloromercuribenzoic acid (PCMB). Enzyme II with a pH optimum of 7 to 8 was more labile, quite sensitive to PCMB and moderately inhibited by chelators. A high-molecular weight arginine aminopeptidase (mol wt. > 200,000) was sensitive to PCMB and showed a value of 0.55 mM for <em>K</em><subscript>m</subscript> in the hydrolysis of <em>N</em>α-L-arginyl-2NA. The hydrolysis of PZ-PLGPA and gelatin suggests that this organism may contain collagenolytic proteinases. Because the insoluble proteinase substrate Azocoll was not hydro1yzed, these enzymes may be active on soluble collagenous substances only. <em>T. vincentii</em> ATCC 35580 typifies an organism rich in PZ-PLGPA-endopeptidase, argimne aimnopeptidase and γ-glutamylpeptidase activity. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 09020055
- Volume :
- 3
- Issue :
- 3
- Database :
- Complementary Index
- Journal :
- Oral Microbiology & Immunology
- Publication Type :
- Academic Journal
- Accession number :
- 12525614
- Full Text :
- https://doi.org/10.1111/j.1399-302X.1988.tb00096.x