Linked Life Data

6801056

Source:http://linkedlifedata.com/resource/pubmed/id/6801056

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1982-5-27
pubmed:abstractText
Xanthine dehydrogenase was purified more than 1500-fold from crude extracts of wild type Drosophila melanogaster. Like the bovine milk and chicken liver enzymes, the purified Drosophila enzyme was inactivated by cyanide, and the cyanide-inactivated desulfo enzyme was reactivated by anaerobic incubation with 1 mM sulfide and 1 mM dithionite. Application of the resulfuration procedure to crude extracts of Drosophila ma-l flies which slow pleiotropic deficiencies of xanthine dehydrogenase, aldehyde oxidase, and pyridoxal oxidase led to the emergence of xanthine dehydrogenase and aldehyde oxidase activities. Representatives of all the five known complementation groups of ma-l mutants were amenable to activation; 59-95% of wild type xanthine dehydrogenase activity and 1-7% of wild type aldehyde oxidase activity were reconstituted. Evidence for the identity of in vitro reconstituted xanthine dehydrogenase from ma-l mutants with wild type enzyme is presented. Since the inactive xanthine dehydrogenase and aldehyde oxidase proteins present in ma-l mutants are identical with the catalytically inactive desulfo forms obtained by cyanide treatment of active enzymes, these data constitute evidence for genetic control of the incorporation of the cyanolyzable sulfur of Mo hydroxylases.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
257
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3958-62
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Drosophila melanogaster ma-l mutants are defective in the sulfuration of desulfo Mo hydroxylases.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't