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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1988-1-13
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pubmed:abstractText |
The action of bovine spleen cathepsin B as a dipeptidyl carboxypeptidase on newly synthesized substrates of the type peptidyl-X-p-nitrophenylalanyl (Phe(NO2))-Y (X,Y = amino acid residue) or 5-dimethylaminonaphthalene-1-sulfonyl (Dns)-peptidyl-X-Phe(NO2)-Y was investigated. The kinetic parameters of hydrolysis of the X-Phe(NO2) bond were determined by difference spectrophotometry (delta epsilon 310 = 1600 M-1 cm-1) or by spectrofluorometry by following the five- to eightfold increase of Dns-group fluorescence with excitation at 350 nm and emission at 535 nm. The substrates were moderately sensitive to cathepsin B; kcat varied from 0.7 to 4 s-1 at pH 5 and 25 degrees C; Km varied from 6 to 240 microM. The very acidic optima of pH 4-5 are characteristic for dipeptidyl carboxypeptidase activity of cathepsin B. Bovine spleen cathepsins S and H had little and no activity, respectively, when assayed with Pro-Glu-Ala-Phe(NO2)-Gly. These peptides should be a valuable tool for routine assays and for mechanistic studies on cathepsin B.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0003-2697
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
165
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
96-101
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:3318552-Cathepsin B,
pubmed-meshheading:3318552-Cathepsin H,
pubmed-meshheading:3318552-Cathepsins,
pubmed-meshheading:3318552-Chromogenic Compounds,
pubmed-meshheading:3318552-Cysteine Endopeptidases,
pubmed-meshheading:3318552-Endopeptidases,
pubmed-meshheading:3318552-Fluorescent Dyes,
pubmed-meshheading:3318552-Hydrogen-Ion Concentration,
pubmed-meshheading:3318552-Hydrolysis,
pubmed-meshheading:3318552-Peptides,
pubmed-meshheading:3318552-Spectrometry, Fluorescence,
pubmed-meshheading:3318552-Spectrophotometry, Ultraviolet
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pubmed:year |
1987
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pubmed:articleTitle |
Chromophoric and fluorophoric peptide substrates cleaved through the dipeptidyl carboxypeptidase activity of cathepsin B.
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pubmed:affiliation |
Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Sciences, Prague.
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pubmed:publicationType |
Journal Article
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