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The peptidolytic capacity of the spirochete system

dc.contributor.authorMäkinen, K. K.en_US
dc.contributor.authorMäkinen, P. -L.en_US
dc.date.accessioned2006-09-08T20:08:03Z
dc.date.available2006-09-08T20:08:03Z
dc.date.issued1996-06en_US
dc.identifier.citationMäkinen, K. K.; Mäkinen, P.-L.; (1996). "The peptidolytic capacity of the spirochete system." Medical Microbiology and Immunology 185(1): 1-10. <http://hdl.handle.net/2027.42/42252>en_US
dc.identifier.issn0300-8584en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/42252
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=8803947&dopt=citationen_US
dc.description.abstract  Relatively scant chemical information has been available on the proteinases and peptidases of spirochetes in spite of the association of spirochetes with several serious infections known to plague humans and other animal species. This situation has partly resulted from difficulties in growing some spirochetes under laboratory conditions. The cells of Treponema denticola , a spirochete suggested to be associated with periodontal infections, have turned out to be a good source of new chemical information on those enzymes. Latest studies suggest that the outer cell en-velope or the periplasmic space of T. denticola contains several novel proteinases and peptidases (hence called ``ectoenzymes'') which may contribute to the chronicity of periodontal infections. Some of the oligopeptidases discovered are specific for proline-containing host tissue peptides such as substance P, bradykinin, neurotensin, etc., and possibly small collagen fragments. The only spirochetal peptidases purified to give a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis have been obtained from T. denticola . One particular peptidase, suggested to be similar to the oligopeptidase B (EC 3.4.21.83) of Escherichia coli seems to be present in the cell envelope or in the periplasmic space at quite large concentrations. The presence of this and several other peptidases in the outer cell structures of the treponemes suggests that such enzymes are important for the nutrition of these highly motile and invasive organisms. The biological role of these enzymes can thus be envisaged in the peptidolytic processing of host tissue proteins and peptides to gradually smaller molecules to fulfill the nutritional requirements of these organisms. Although the genetic similarity between T. denticola and some other treponemes and spirochetes can be hotly debated, it is nevertheless now possible to use T. denticula enzymes as suitable objects for comparison when the chemistry of other spirochetes is studied.en_US
dc.format.extent341114 bytes
dc.format.extent3115 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherSpringer-Verlag; Springer-Verlag Berlin Heidelbergen_US
dc.subject.other Treponemes en_US
dc.subject.otherKey Words  Spirochetes en_US
dc.subject.otherLegacyen_US
dc.subject.other Peptidases en_US
dc.subject.other Proteinases en_US
dc.subject.other Treponemal Infectionsen_US
dc.titleThe peptidolytic capacity of the spirochete systemen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelPublic Healthen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biologic and Materials Sciences, School of Dentistry, The University of Michigan, Ann Arbor, MI 48109, USA Tel.: 1-313-761-7317; Fax: 1-313-747-3896, USen_US
dc.contributor.affiliationumDepartment of Biologic and Materials Sciences, School of Dentistry, The University of Michigan, Ann Arbor, MI 48109, USA Tel.: 1-313-761-7317; Fax: 1-313-747-3896, USen_US
dc.contributor.affiliationumcampusAnn Arboren_US
dc.identifier.pmid8803947en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/42252/1/430-185-1-1_61850001.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1007/s004300050008en_US
dc.identifier.sourceMedical Microbiology and Immunologyen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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