Switch to
Predicate | Object |
---|---|
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-meshheading:1181268-Animals,
pubmed-meshheading:1181268-Cattle,
pubmed-meshheading:1181268-Chymotrypsin,
pubmed-meshheading:1181268-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1181268-Enzyme Activation,
pubmed-meshheading:1181268-Kinetics,
pubmed-meshheading:1181268-Macroglobulins,
pubmed-meshheading:1181268-Mathematics,
pubmed-meshheading:1181268-Molecular Weight
|
pubmed:year |
1975
|
pubmed:articleTitle |
The effect of alpha2-macroglobulin from bovine serum on bovine alpha-chymotrypsin.
|
pubmed:publicationType |
Journal Article
|