Linked Life Data

3820185

Source:http://linkedlifedata.com/resource/pubmed/id/3820185

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1987-3-31
pubmed:abstractText
Cathepsin B (EC 3.4.22.1) has been purified from rabbit testes to apparent homogeneity by chromatography on DE-52, affinity chromatography on organomercurial agarose and subsequent gel filtrations on Sephadex G-75. The enzyme is composed of a single polypeptide of Mr 23,000. Thiol blocking agents and leupeptin abolished the activity of the enzyme completely. The enzyme showed maximum activity at pH 6.0 and 43 degrees C, required 2 mM-cysteine for the optimal activity and had a Km1.45 X 10(-3) M using Z-Arg-beta-naphthylamide as the substrate. However, Z-Arg-Arg-beta-naphthylamide was 12 times more sensitive as a substrate than was Z-Arg-beta-naphthylamide. Rabbit testicular cathepsin B hydrolysed intact proteins. An endogenous inhibitor isolated from the rabbit testes inhibited purified Cathepsin B.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0022-4251
pubmed:author
pubmed:issnType
Print
pubmed:volume
79
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
67-74
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Isolation and characterization of cathepsin B from rabbit testis.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.