Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1979-10-17
pubmed:abstractText
We find from studying the inhibitory effect of N-ethylmaleimide (NEM) on the enzymatic activity of beta-hydroxybutyrate dehydrogenase, that approximately one molecule of NEM is bound for one molecule of protein when the enzymatic activity is completely inhibited. Since the protein is a dimer this implies that each molecule of protein possesses only one thiol group in its catalytic center. Two long chain maleimide derivates: (10.3) NEM and (1.14) NEM conform, if a reasonable assumption is accepted to the conditions required for the study of the recombination of beta-hydroxybutyrate dehydrogenase with lecithin vesicles by spin label technique.
pubmed:language
fre
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0567-655X
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
288
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
363-5
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
[Choice of a spin label probe in order to study the recombination of beta-hydroxybutyrate dehydrogenase of a rat liver inner mitochondrial membrane with lecithin vesicles].
pubmed:publicationType
Journal Article, English Abstract