Show simple item record

Biochemical comparison of proteolytic enzymes present in rough- and smooth-surfaced capnocytophagas isolated from the subgingival plaque of periodontitis patients

dc.contributor.authorSöderling, E.en_US
dc.contributor.authorMäkinen, P. L.en_US
dc.contributor.authorSyed, S.en_US
dc.contributor.authorMäkinen, K. K.en_US
dc.date.accessioned2010-04-01T15:18:23Z
dc.date.available2010-04-01T15:18:23Z
dc.date.issued1991-01en_US
dc.identifier.citationSÖderling, E.; MÄkinen, P. L.; Syed, S.; MÄkinen, K. K. (1991). "Biochemical comparison of proteolytic enzymes present in rough- and smooth-surfaced capnocytophagas isolated from the subgingival plaque of periodontitis patients." Journal of Periodontal Research 26(1): 17-23. <http://hdl.handle.net/2027.42/65779>en_US
dc.identifier.issn0022-3484en_US
dc.identifier.issn1600-0765en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/65779
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=1825330&dopt=citationen_US
dc.format.extent3690557 bytes
dc.format.extent3110 bytes
dc.format.mimetypeapplication/octet-stream
dc.format.mimetypetext/plain
dc.publisherBlackwell Publishing Ltden_US
dc.rightsMunksgaard 1991en_US
dc.subject.otherPeriodontitisen_US
dc.subject.otherProteolytic Enzymesen_US
dc.subject.otherCapnocytophagaen_US
dc.titleBiochemical comparison of proteolytic enzymes present in rough- and smooth-surfaced capnocytophagas isolated from the subgingival plaque of periodontitis patientsen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelDentistryen_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, Michigan, U.S.A.en_US
dc.identifier.pmid1825330en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/65779/1/j.1600-0765.1991.tb01621.x.pdf
dc.identifier.doi10.1111/j.1600-0765.1991.tb01621.xen_US
dc.identifier.sourceJournal of Periodontal Researchen_US
dc.identifier.citedreferenceAlfano NC, Chasen Al, Nasi CW. Autodiographic study of the penetration of dextrans and insulin through nonkeratinized oral mucosa in vitro ? J Periodont Res 1977 ; 12 : 368 – 72.en_US
dc.identifier.citedreferenceBick PH, Belts Carpenter A, Holdeman LV, et al. Polyclonal B-cell activation induced by extracts of gram-negative bacteria isolated from periodontally diseased sites. Infect Immun 1981 ; 34 : 43 – 9.en_US
dc.identifier.citedreferenceBond MD, Van Wart HE. Purification and separation of individual collagenases of Clostridium histolyticum using red dye ligand chromatography. Biochemistry 1984 ; 23 : 3077 – 85.en_US
dc.identifier.citedreferenceBradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976 ; 72 : 248 – 54.en_US
dc.identifier.citedreferenceDoi E, Shibata D, Matoba T. Modified colorimetric ninhydrin methods for peptidase assay. Anal Biochem 1981 ; 118 : 173 – 84.en_US
dc.identifier.citedreferenceFinegold SM. Anaerobic bacteria in human disease. New York : Academic Press Inc., 1977.en_US
dc.identifier.citedreferenceHanks CT, Kim J-S, Edwards CA. Growth control of cultured rat calvarium cells by platelet-derived growth factor. J Oral Pathol 1986 ; 15 : 476 – 83.en_US
dc.identifier.citedreferenceKilian M. Degradation of immunoglobulins Al, A2, and G by suspected principal periodontal pathogens. Infect Immun 1981 ; 34 : 757 – 65.en_US
dc.identifier.citedreferenceLaughon BE, Syed SA, Loesche WJ. API ZYM system for identification of Bacteroides spp., Capnocytophaga spp., and spirochetes of oral origin. J Clin Microbiol 1982 ; 15 : 97 – 102.en_US
dc.identifier.citedreferenceLoesche WJ. The identification of bacteria associated with periodontal disease and dental caries by enzymatic methods. Oral Microbiol Immunol 1986 ; 1 : 65 – 70.en_US
dc.identifier.citedreferenceMashimo PA, Yamamoto Y, Slots J, Park BH, Genco RJ. The periodontal microflora of juvenile diabetics: Culture, immunofluorescence, and serum antibody studies. J Periodontol 1983 ; 54 : 420 – 30.en_US
dc.identifier.citedreferenceMÄkinen KK, MÄkinen P-L. Purification and characterization of two human erythrocyte arylamidases preferentially hydrolysising N-terminal arginine or lysine residues. Biochem J 1978 ; 175 : 1051 – 67.en_US
dc.identifier.citedreferenceMÄkinen KK, Syed SA, Loesche WJ, MÄkinen P-L. Proteolytic profile of Treponema vincentii ATCC 35580 with special reference to collagenolytic and arginine aminopeptidase activity. Oral Microbiol Immunol 1988 ; 3 : 121 – 8.en_US
dc.identifier.citedreferenceMÄkinen KK, Syed SA, MÄkinen P-L, Loesche WJ. Benzoylarginine peptidase and iminopeptidase profiles of Treponema denticola strains isolated from the human periodontal pocket. Curr Microbiol 1986 ; 14 : 85 – 9.en_US
dc.identifier.citedreferenceNakamura M, Slots J. Aminopeptidase activity of Capnocytophaga ? J Periodont Res 1982 ; 17 : 597 – 603.en_US
dc.identifier.citedreferenceSaglie R, Carranza FA Jr, Newman MG, et al. Microscopic, cultural, and immunologic methods for identification of bacteria within human periodontal tissues. IADR Program Abstracts of Papers 1983 ( Abstract No. 78 ), p. 178.en_US
dc.identifier.citedreferenceSchwartz J, Stinson FL, Parker RB. The passage of tritiated bacterial endotoxin across intact gingival crevicular epithelium. J Periodontol 1972 ; 43 : 270 – 5.en_US
dc.identifier.citedreferenceSlots J. Subgingival microflora and periodontal disease. J Clin Periodontol 1979 ; 6 : 351 – 82.en_US
dc.identifier.citedreferenceSlots J. Enzymatic characterization of some oral and nonoral gram-negative bacteria with the API ZYM system. J Clin Microbiol 1981 ; 14 : 288 – 94.en_US
dc.identifier.citedreferenceSlots J, Genco RJ. Black-pigmented Bacteroides species, Capnocytophaga species, and Actinobacillus actinomycetemcomitans in human periodontal disease: virulence factors in colonization, survival, and tissue destruction. J Dent Res 1984 ; 63 : 412 – 21.en_US
dc.identifier.citedreferenceSteffen EK, Hentges DJ. Hydrolytic enzymes of anaerobic bacteria isolated from human infections. J Clin Microbiol 1981 ; 14 : 153 – 6.en_US
dc.identifier.citedreferenceTanner ACR, Strzempko MN, Belsky CA, McKinley GA. API ZYM and API An-Ident reaction of fastidious oral gram-negative species. J Clin Microbiol 1985 ; 22 : 333 – 5.en_US
dc.identifier.citedreferenceUitto V-J, Haapasalo M, Laakso T, Salo T. Degradation of basement membrane collagen by proteases from some anaerobic oral microorganisms. Oral Microbiol Immunol 1988 ; 3 : 97 – 102.en_US
dc.identifier.citedreferenceVan Dyke TE, Bartholomew E, Genco RJ, Slots J, Levine MJ. Inhibition of neutrophil chemotaxis by soluble bacterial products. J Periodontol 1982 ; 53 : 502 – 8.en_US
dc.identifier.citedreferenceVan Wart HE, Steinbrink DE. A continuous spechrophotometric assay for Clostridium histolyticum collagenase. Anal Biochem 1981 ; 113 : 356 – 65.en_US
dc.identifier.citedreferenceWÜnsch E, Heidrich HG. Quantitative Bestimmung der Kollagenase. Hoppe-Seyler's Z Physiol Chem 1963 ; 333 : 149 – 51.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


Files in this item

Show simple item record

Remediation of Harmful Language

The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.

Accessibility

If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.