Linked Life Data

454646

Source:http://linkedlifedata.com/resource/pubmed/id/454646

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1979-9-17
pubmed:abstractText
Rat muscle was extracted at pH 4 and submitted to gel-filtration on Sephadex G-75 and to chromatography on DEAE-Sephadex. Gel-filtration gave a large peak of activity towards Bz-Arg-NNap with an estimated molecular weight of 25,500. Activity towards Bz-Arg-NH2 was present in this peak and in another peak of molecular weight 45,000. The second peak also hydrolysed benzoyl-glycyl-L-arginine. DEAE-Sephadex gave five peaks of Bz-Arg-NNap hydrolysing activity; all showed thiol dependence. Peaks III, IV and V hydrolysed Z-Ala-Arg-Arg-NNap-OMe rapidly; they also inactivated aldolase and were strongly inhibited by leupeptin. They are probably isoenzymes of cathepsin B1. Peak I showed these properties to a relatively small extent. 7-(N-Benzoyl-DL-argininamide)-4-methylcoumarin appears to be an alternative substrate for cathepsin B1; it was hydrolysed also by peak I, but relatively less rapidly. Peaks I and II were inhibited more than peaks III, IV and V by a muscle extract. Total activity of the Bz-Arg-NH2-hydrolysing enzyme in extensor digitorum longus muscle increased after denervation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
577
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
253-66
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Separation of cathepsin B1 and related enzymes from rat skeletal muscle.
pubmed:publicationType
Journal Article