Hydrolysis of the Leu-Gly bond of phenylazobenzyl-oxycarbonyl- l -Pro- l -Leu-Gly- l -Pro- D -Arg (a substrate of microbial collagenases) by treponemes isolated from the subgingival plaque of periodontitis patients
dc.contributor.author | Mäkinen, Kauko K. | en_US |
dc.contributor.author | Syed, Salam A. | en_US |
dc.contributor.author | Salvador, Sergio L. | en_US |
dc.contributor.author | Mäkinen, Pirkko-Liisa | en_US |
dc.date.accessioned | 2006-09-08T19:08:49Z | |
dc.date.available | 2006-09-08T19:08:49Z | |
dc.date.issued | 1990-01 | en_US |
dc.identifier.citation | Mäkinen, Kauko K.; Syed, Salam A.; Salvador, Sergio L.; Mäkinen, Pirkko-Liisa; (1990). "Hydrolysis of the Leu-Gly bond of phenylazobenzyl-oxycarbonyl- l -Pro- l -Leu-Gly- l -Pro- D -Arg (a substrate of microbial collagenases) by treponemes isolated from the subgingival plaque of periodontitis patients." Current Microbiology 20(1): 69-74. <http://hdl.handle.net/2027.42/41336> | en_US |
dc.identifier.issn | 1432-0991 | en_US |
dc.identifier.issn | 0343-8651 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/41336 | |
dc.description.abstract | Cell extracts prepared from several oral treponemes isolated from the subgingival plaque of periodontitis patients showed high enzyme activity toward phenylazobenzyl-oxycarbonyl- l -prolyl- l -leucylglycyl- l -prolyl- d -arginine (a compound used as a substrate for microbial collagenases). One major enzyme hydrolyzing this substrate at the Leu-Gly bond only was partially purified from an unspeciated treponeme (strain US), Treponema denticola ATCC 35405, and 29 different clinical isolates of T. denticola . The Treponema US enzyme also hydrolyzed furylacryloyl- l -leucylglycyl- l -prolyl- l -alanine (another substrate of bacterial collagenases) at the Leu-Gly bond. This enzyme also hydrolyzed various collagens and collagen-derived peptides. These treponemal proteases were sensitive to metal chelators and p -chloromercury compounds. The results indicate that human oral treponemes contain enzymes that readily hydrolyze in chromogenic protease substrates the Leu-Gly bond only that is the cleavage site of these substrates also by “true” microbial collagenases. | en_US |
dc.format.extent | 660911 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Springer-Verlag; Springer-Verlag New York Inc. | en_US |
dc.subject.other | Biotechnology | en_US |
dc.subject.other | Life Sciences | en_US |
dc.subject.other | Microbiology | en_US |
dc.title | Hydrolysis of the Leu-Gly bond of phenylazobenzyl-oxycarbonyl- l -Pro- l -Leu-Gly- l -Pro- D -Arg (a substrate of microbial collagenases) by treponemes isolated from the subgingival plaque of periodontitis patients | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biologic and Materials Sciences, School of Dentistry, The University of Michigan, Ann Arbor, Michigan, USA | en_US |
dc.contributor.affiliationum | Department of Biologic and Materials Sciences, School of Dentistry, The University of Michigan, Ann Arbor, Michigan, USA | en_US |
dc.contributor.affiliationum | Department of Biologic and Materials Sciences, School of Dentistry, The University of Michigan, Ann Arbor, Michigan, USA | en_US |
dc.contributor.affiliationum | Department of Biologic and Materials Sciences, School of Dentistry, The University of Michigan, Ann Arbor, Michigan, USA | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/41336/1/284_2005_Article_BF02094028.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1007/BF02094028 | en_US |
dc.identifier.source | Current Microbiology | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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