Linked Life Data

223627

Source:http://linkedlifedata.com/resource/pubmed/id/223627

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1979-10-26
pubmed:abstractText
Mitochondrial aspartate aminotransferase, an enzyme localized on the inner face of the inner mitochondrial membrane, is released into the intermembrane space upon addition of a "movement effector" (succinate, fumarate, pyruvate, or glutamate) [Waksman, A., & Rendon, A. (1974) Biochimie 56, 907-924]. After removal of the movement effector, 90% of the released enzyme rebound to mitoplasts. Lubrol fractionation showed that this bound activity was associated with the inner membrane. Internalization was demonstrated by using both enzymatic and molecular approaches. It was found that 70% of the reassociated enzyme became inaccessible from the outside of the mitoplast either to a nonpermeating substrate (NADH), to mild protease hydrolysis, or to recognition by a specific antibody. In contrast, in inside-out vesicles, the enzyme remained accessible to NADH, protease, and antibodies. Latency measurements performed at different temperatures on whole intact mitochondria confirmed the existence of reversible intermembrane movement of the enzyme in situ.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3119-26
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Direct evidence for internalization of mitochondrial aspartate aminotransferase into mitoplasts.
pubmed:publicationType
Journal Article, In Vitro