Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1976-8-2
pubmed:abstractText
Glutamate-glyoxylate aminotransferase which mediates the reaction of glyoxylic acid with glutamic acid to yield glycine and alpha-oxoglutaric acid has been isolated and purified 84-fold from extracts of Lactobacillus plantarum. Purified enzyme requires the addition of pyridoxal phosphate and magnesium ions for its activity. The molecular weight of the enzyme estimated by Sepharose 4B gel filtration amounts to 37.000. Micaelis constants for glyoxylate and glutamate are corresponding to 6.25 X 10(-3) M and 2.75 X 10(-3) M, respectively. Optimal pH in phosphate and veronal buffers is 8.0 and optimal temperature 35--37 degrees C.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0567-7823
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
243-52
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
L-Glutamate-glyoxylate aminotransferase in Lactobacillus plantarum.
pubmed:publicationType
Journal Article