rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1990-1-23
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pubmed:abstractText |
Crevicular fluid samples were collected from 20 gingivitis and periodontitis patients using filter paper strips; these were then eluted into buffer. Portions of each sample were combined and the activities of this pooled eluate against different peptidyl derivatives of 7-amino-4-trifluoromethyl coumarin (AFC) were examined with respect to their pH profiles and effector responses. Ca-thepsin B- and L-like activity was detected with Bz-Val-Lys-Lys-Arg-AFC; elastase-like activity with MeOSuc-Ala-Ala-Pro-Val-AFC; tryptase-like activity with Z-Ala-Ala-Lys-AFC; trypsin-like activity with Z-Gly-Gly-Arg-AFC; and dipeptidyl peptidase (DPP) IV-like activity with Ala-Pro-AFC. The selectivity and sensitivity of these assays were improved by choice of appropriate conditions. The cathepsin B- and L-, elastase-, tryptase-, and trypsin-like activities all had properties consistent with those from host sources, whilst partial inactivation of the DPP IV-like activity by heat treatment (60 degrees C for 30 min) suggested that it may have represented a mixture of human and Bacteroides gingivalis enzymes. Individual patient eluates showed wide variations in enzyme concentrations, but generally elastase-like activity was by far the highest. The sensitivity of the assays with AFC-linked substrates was such that it should prove possible to measure all five different types of activity in crevicular fluid samples from local periodontal disease sites.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
D
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/7-amino-4-trifluoromethylcoumarin,
http://linkedlifedata.com/resource/pubmed/chemical/CTSL1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin B,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin L,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsins,
http://linkedlifedata.com/resource/pubmed/chemical/Coumarins,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Dipeptidyl Peptidase 4,
http://linkedlifedata.com/resource/pubmed/chemical/Dipeptidyl-Peptidases and...,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Pancreatic Elastase,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/tosylarginine methyl ester hydrolase
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0022-3484
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
24
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
353-61
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:2574234-Amino Acid Sequence,
pubmed-meshheading:2574234-Cathepsin B,
pubmed-meshheading:2574234-Cathepsin L,
pubmed-meshheading:2574234-Cathepsins,
pubmed-meshheading:2574234-Coumarins,
pubmed-meshheading:2574234-Cysteine Endopeptidases,
pubmed-meshheading:2574234-Dipeptidyl Peptidase 4,
pubmed-meshheading:2574234-Dipeptidyl-Peptidases and Tripeptidyl-Peptidases,
pubmed-meshheading:2574234-Endopeptidases,
pubmed-meshheading:2574234-Enzyme Activation,
pubmed-meshheading:2574234-Gingival Crevicular Fluid,
pubmed-meshheading:2574234-Gingivitis,
pubmed-meshheading:2574234-Hot Temperature,
pubmed-meshheading:2574234-Humans,
pubmed-meshheading:2574234-Hydrogen-Ion Concentration,
pubmed-meshheading:2574234-Molecular Sequence Data,
pubmed-meshheading:2574234-Pancreatic Elastase,
pubmed-meshheading:2574234-Peptide Hydrolases,
pubmed-meshheading:2574234-Periodontitis,
pubmed-meshheading:2574234-Substrate Specificity,
pubmed-meshheading:2574234-Trypsin
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pubmed:year |
1989
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pubmed:articleTitle |
Detection of cathepsin B- and L-, elastase-, tryptase-, trypsin-, and dipeptidyl peptidase IV-like activities in crevicular fluid from gingivitis and periodontitis patients with peptidyl derivatives of 7-amino-4-trifluoromethyl coumarin.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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