Linked Life Data

3522589

Source:http://linkedlifedata.com/resource/pubmed/id/3522589

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
1986-8-13
pubmed:abstractText
The major cathepsin B isozyme CB-I purified from porcine spleens was studied for its specificity against various peptide and denatured protein substrates. The enzyme degraded all the peptide substrates by an exopeptidase activity. The substrates were degraded mainly by a dipeptidyl carboxypeptidase activity of the enzyme except for angiotensin I, from which a COOH-terminal leucine residue was released. The enzyme failed to hydrolyze peptides having a proline or cysteic acid in the COOH-terminal, penultimate, and antepenultimate positions. Reduced and carboxymethylated soybean trypsin inhibitor was degraded by the same dipeptidyl carboxypeptidase action of cathepsin B. No significant endopeptidase activity was observed. These results do not support the general assumption that cathepsin B has both endo- and exopeptidase activities, neither do these observations support the postulation that cathepsin B might be involved in the in vivo proteolytic processing of protein precursors. We propose that the biological role of this enzyme is mainly the degradation of tissue proteins in lysosomes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
261
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9375-81
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Porcine spleen cathepsin B is an exopeptidase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.