Linked Life Data

7113549

Source:http://linkedlifedata.com/resource/pubmed/id/7113549

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1982-10-12
pubmed:abstractText
A thiol proteinase inhibitor was purified from rat liver by a rapid procedure involving heat treatment of the post-lysosomal fraction, affinity chromatography on papain-Sepharose 4B and Sephadex G-75. The purified inhibitor appeared homogeneous on sodium dodecyl sulfate electrophoresis. The inhibitor had a molecular weight of about 11000 and consists of three forms (pI 4.9, 5.2 and 5.6). The preparation inhibited thiol proteinases but not serine proteinase or aspartate proteinase. Kinetic studies of inhibition of papain by the inhibitor indicate that the inhibition was noncompetitive and pseudo-irreversible. Subcellular fractionations of rat liver indicate that most of all the inhibitor is localized in the cytosol fraction. The physiological role of the inhibitor is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0001-5318
pubmed:author
pubmed:issnType
Print
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
69-74
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Endogenous thiol proteinase inhibitor from rat liver.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't