| pubmed-article:3318552 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3318552 | lifeskim:mentions | umls-concept:C0699919 | lld:lifeskim |
| pubmed-article:3318552 | lifeskim:mentions | umls-concept:C0205242 | lld:lifeskim |
| pubmed-article:3318552 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:3318552 | lifeskim:mentions | umls-concept:C1150210 | lld:lifeskim |
| pubmed-article:3318552 | lifeskim:mentions | umls-concept:C0058360 | lld:lifeskim |
| pubmed-article:3318552 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:3318552 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:3318552 | pubmed:dateCreated | 1988-1-13 | lld:pubmed |
| pubmed-article:3318552 | 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. | lld:pubmed |
| pubmed-article:3318552 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3318552 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3318552 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3318552 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3318552 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3318552 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3318552 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3318552 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3318552 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3318552 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3318552 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3318552 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3318552 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3318552 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3318552 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:3318552 | pubmed:issn | 0003-2697 | lld:pubmed |
| pubmed-article:3318552 | pubmed:author | pubmed-author:PohlJJ | lld:pubmed |
| pubmed-article:3318552 | pubmed:author | pubmed-author:StroeEE | lld:pubmed |
| pubmed-article:3318552 | pubmed:author | pubmed-author:KostkaVV | lld:pubmed |
| pubmed-article:3318552 | pubmed:author | pubmed-author:BláhaII | lld:pubmed |
| pubmed-article:3318552 | pubmed:author | pubmed-author:DavinicSS | lld:pubmed |
| pubmed-article:3318552 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3318552 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:3318552 | pubmed:volume | 165 | lld:pubmed |
| pubmed-article:3318552 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3318552 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3318552 | pubmed:pagination | 96-101 | lld:pubmed |
| pubmed-article:3318552 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:3318552 | pubmed:meshHeading | pubmed-meshheading:3318552-... | lld:pubmed |
| pubmed-article:3318552 | pubmed:meshHeading | pubmed-meshheading:3318552-... | lld:pubmed |
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| pubmed-article:3318552 | pubmed:meshHeading | pubmed-meshheading:3318552-... | lld:pubmed |
| pubmed-article:3318552 | pubmed:meshHeading | pubmed-meshheading:3318552-... | lld:pubmed |
| pubmed-article:3318552 | pubmed:meshHeading | pubmed-meshheading:3318552-... | lld:pubmed |
| pubmed-article:3318552 | pubmed:meshHeading | pubmed-meshheading:3318552-... | lld:pubmed |
| pubmed-article:3318552 | pubmed:meshHeading | pubmed-meshheading:3318552-... | lld:pubmed |
| pubmed-article:3318552 | pubmed:meshHeading | pubmed-meshheading:3318552-... | lld:pubmed |
| pubmed-article:3318552 | pubmed:meshHeading | pubmed-meshheading:3318552-... | lld:pubmed |
| pubmed-article:3318552 | pubmed:meshHeading | pubmed-meshheading:3318552-... | lld:pubmed |
| pubmed-article:3318552 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3318552 | pubmed:articleTitle | Chromophoric and fluorophoric peptide substrates cleaved through the dipeptidyl carboxypeptidase activity of cathepsin B. | lld:pubmed |
| pubmed-article:3318552 | pubmed:affiliation | Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Sciences, Prague. | lld:pubmed |
| pubmed-article:3318552 | pubmed:publicationType | Journal Article | lld:pubmed |
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