Linked Life Data

6393951

Source:http://linkedlifedata.com/resource/pubmed/id/6393951

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9-10
pubmed:dateCreated
1985-2-5
pubmed:abstractText
Zymograms of Arabidopsis alcohol dehydrogenase (ADH; EC 1.1.1.1) show a unique anodal migrating band. Three electrophoretic variants were identified among geographical races and designated slow (S), fast (F), and superfast (A), according to their mobility on Tris-citrate starch gels. In plants ADH activity is confined mainly to pollen, seeds, and grains and rapidly declines during the germination process. In callus and suspension cultures, growing on media containing 2,4-D, ADH appeared as one of the major polypeptides. Genetical analysis indicated that the three types of ADH isozymes are under the control of one gene with three alles (Adh1S, Adh1F, Adh1A), showing codominant expression. Crosses between the electrophoretic types and dissociation-reassociation experiments showed that the Arabidopsis enzyme behaves as a dimer, like ADH from most other species. The molecular weight of the enzyme has been estimated by gel filtration and by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis to be 87,000. The pH optimum for the oxidation of ethanol is 9.0 and two optima for reduction of acetaldehyde have been obtained, 6.0 and 8.5, respectively. The enzyme exhibits a wide substrate specificity for alcohols and is relatively heat resistant.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2928
pubmed:author
pubmed:issnType
Print
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
817-38
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Polymorphism of alcohol dehydrogenase in Arabidopsis thaliana (L.) Heynh.: genetical and biochemical characterization.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't