Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
1981-12-15
pubmed:abstractText
Alanine: gamma, delta-dioxovalerate aminotransferase had been purified from bovine liver mitochondria, and the capacity of this enzyme to form delta-aminolevulinic acid had been suggested to be far greater than that of delta-aminolevulinate synthase (EC 2.3.1.37) from the same mitochondria (Varticovski, L., Kushner, J. P., and Burnham, B. F. (1980) J. Biol. Chem. 255, 3742-3747). In the present study, alanine: gamma, delta-dioxovalerate aminotransferase and alanine-glyoxylate aminotransferase (EC 2.6.1.44) were co-purified to homogeneity from bovine liver mitochondria. The ratio of the two activities remains constant during purification and is unchanged by a variety of treatments of the purified enzyme. Alanine: gamma, delta-dioxovalerate aminotransferase activity is competitively inhibited by glyoxylate. Some kinetic data are presented. These results show that the two activities are associated with the same protein. The enzyme is much higher in the glyoxylate aminotransferase activity than in the dioxovalerate aminotransferase activity. The purified enzyme has a molecular weight of approximately 240,000 with four identical subunits and an isoelectric point of 5.4. The ratio of the gamma, delta-dioxovalerate aminotransferase activity to the glyoxylate aminotransferase was determined with alanine:glyoxylate aminotransferase preparations from various mammalian liver and kidney.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10335-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Biosynthesis of porphyrin precursors in mammals. Identity of alanine: gamma, delta-dioxovalerate aminotransferase with alanine:glyoxylate aminotransferase.
pubmed:publicationType
Journal Article, Comparative Study