Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1976-1-8
pubmed:abstractText
Bovine alpha2-globulin contains a protein which increases the activity of bovine alpha-chymotrypsin against synthetic substrates. The active protein fraction migrates slowly on polyacrylamide gel electrophoresis, so it was named slow alpha2-globulin (Salpha2). The fraction was isolated from bovine serum and purified. Its sedimentation constant S20 was 18.5 S. It was thus identified with the alpha2-macroglobulin (alpha2M). By kinetic studies, the dissociation constant of the alpha-chymotrypsin-alpha2 M complex was calculated to be of the order of 10(-7) l/mol. The purified alpha2 M was shown to bind alpha-chymotrypsin at a definite rate. If the binding ratio was assumed to be 1:2, the molecular weight was calculated to be about 8 X 10(5).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0018-4888
pubmed:author
pubmed:issnType
Print
pubmed:volume
356
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
677-92
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
The effect of alpha2-macroglobulin from bovine serum on bovine alpha-chymotrypsin.
pubmed:publicationType
Journal Article