Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1982-12-2
pubmed:abstractText
A method for the purification of canine hepatic lipase from post-heparin hepatic venous blood plasma was developed and found applicable to mixed venous post-heparin plasma. The method employs sequential (NH4)2SO4 fractionation, heparin-Sepharose chromatography at pH 8.8 and, finally, adsorption to antiserum prepared against dog pre-heparin plasma. The lipase was purified 10,000-fold. The specific activity assayed with Intralipid as substrate was 840 mumol free fatty acid h-1 . mg-1. Enzyme recovery was 20%. Upon electrophoresis of the purified lipase in polyacrylamide gel containing SDS, a major protein-staining band with an apparent molecular weight of 60,000 was consistently found. This component accounted for 85-90% of the protein applied to the gel, and by amino acid analysis appeared to be distinct from canine antithrombin III, a protein thought to contaminate hepatic lipase purified by earlier methods.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
712
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
71-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Purification of canine post-heparin hepatic lipase.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.