Linked Life Data

7004492

Source:http://linkedlifedata.com/resource/pubmed/id/7004492

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-3-27
pubmed:abstractText
delta 1-Pyrroline-5-carboxylate reductase (L-proline:NAD(P)+ 5-oxidoreductase, EC 1.5.1.2) from Baker's yeast has been purified and characterized. Purification to an apparently homogenous protein was effected by using 'reagent-grade' water containing dithiothreitol and by maintaining a constant pH 7.5, because of the instability of the enzyme protein. The enzyme was purified approximately 200-fold from the crude extract of baker's yeast, and it is a negatively-charged protein with a molecular weight of 125 000, containing an active SH group which participates in binding with NAD(P)H. The Km value for DL-pyrroline-5-carboxylate is 0.8 x 10(-4) M; for NADH, it is 4.8 x 10(-5) M; and for NADPH, it is 5.6 x 10(-5) M. These Km values are much smaller than those of enzymes from other sources. The purified enzyme is free of contaminating enzymes which might interfere with its use in assays. The enzyme has been applied successfully to the assays of L-delta 1-pyrroline-5-carboxylate and L-ornithine in tissue, and in vivo levels of these amino acids in rat liver are reported.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
613
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
318-23
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
delta 1-Pyrroline-5-carboxylate reductase from Baker's yeast. Purification, properties and its application in the assays of L-delta 1-pyrroline-5-carboxylate and L-ornithine in tissue.
pubmed:publicationType
Journal Article