Linked Life Data

1101965

Source:http://linkedlifedata.com/resource/pubmed/id/1101965

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1976-1-8
pubmed:abstractText
Three forms of NAD-dependent alcohol dehydrogenase have been characterized in yeast by their heat sensitivity, their specificity and their electrophoretic patterns. Thermal stability increases in the following order: alcohol dehydrogenase I (fermentative enzyme), alcohol dehydrogenase II (oxidative enzyme), alcohol dehydrogenase III (mitochondrial enzyme). Work with isolated mitochondria shows that alcohol dehydrogenase III is the only form of alcohol dehydrogenase present in these organelles. Starch gel electrophoresis of alcohol dehydrogenase III reveals an active zone of slow migration which consists of five sub-bands. The relative activity of these five sub-bands varies with the conditions of growth. Mitochondrial alcohol dehydrogenase represents never more than 10% of the total cellular alcohol dehydrogenase. Information for its biosynthesis seems to be located in nucleic DNA. The mitochondrial enzyme shows a high affinity for alcohols with a double bond conjugated to the alcohol function.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
405
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
500-12
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Multiple forms of mitochondrial alcohol dehydrogenase in Saccharomyces cerevisiae.
pubmed:publicationType
Journal Article