Linked Life Data

39723

Source:http://linkedlifedata.com/resource/pubmed/id/39723

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1979-12-27
pubmed:abstractText
The mechanisn of hydrolysis of acetylsalicylate during absorption from the gastrointestinl tract has been investigated by identification, quantitation, and purification of a hydrolase from gastric mucosal homogenates. The hydrolase was found to be a soluble, cytosolic enzyme with a pH optimum in the slightly alkaline range, pH 8.6 Acetylsalicylate hydrolase activity was purified from the 100,000 g supernatant fraction by differential (NH4)2SO4 fractionation followed by DEAE-cellulose ion-exchange chromatography and Sephadex or Sephacryl gel filtration. The activity could also be fractionated on hydroxylapatite. The Sephadex-purified fraction containing peak enzyme activity gave a single protein band on SDS-polyacrylamide gel electrophoresis. The molecular weight of the acetylsalicylate hydrolase was 66,400 based on SDS-polyacrylamide gel electrophoresis of the Sephadex-purified enzyme and 59,000 based on gel filtration. By use of the technique described, acetylsalicylate hydrolase can be purified over 100-fold to a specific activity of 10.6 mumol . mg-1 . min-1.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0090-9556
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
215-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Acetylsalicylate hydrolase of rabbit gastric mucosa. Isolation and purification.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, Non-P.H.S.