Linked Life Data

6350043

Source:http://linkedlifedata.com/resource/pubmed/id/6350043

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1983-10-21
pubmed:abstractText
Three cysteine proteinases were isolated from the post-myofibrillar fraction of rat skeletal muscle. Proteinase I preferentially hydrolyzes Z-Phe-Arg-NMec with pH optimum at 8-9. The enzyme activity is stabilized by ATP against thermal inactivation. Proteinase II and III were not resolved by anion-exchange chromatography, by affinity chromatography on Arginine-Sepharose or by gel filtration. Proteinase II, splitting Bz-Val-Gly-Arg-NMec optimally at pH 10-10.5, is inactivated by ATP, whereas Proteinase III, hydrolyzing Suc-Ala-Phe-NMec at pH 7-7.5 is not affected by the nucleotide. The molecular mass of proteinase I is about 750 000 and that of proteinase II and III is about 650 000, as determined by gel filtration.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
160
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
243-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Identification of three high molecular mass cysteine proteinases from rat skeletal muscle.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't