Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1978-1-27
pubmed:abstractText
An acyl-CoA-L-alpha-glycerophosphate acyltransferase system has been found in the fat body of the locust Schistocerca gregaria (Forskäl). After homogenization and differential centrifugation the enzyme system has been localized in two distinct particulate fractions. In both fractions phosphatidic acid was the main reaction product. The 10 000 g -30 000 g particulate fraction was further studied. The enzyme system is very sensitive to pH and Mg2+ concentration. An apparent Km of 0.3-0.5 mM for glycerophosphate was measured. The substrate concentration curve for palmitoyl-CoA is influenced by the protein concentration in the assay medium. This effect would partly explain the non-lineariy of the acylation reactions with respect to enzyme concentration. These observations are correlated with physiological phenomena.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0008-4018
pubmed:author
pubmed:issnType
Print
pubmed:volume
55
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1166-70
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Isolation and properties of a glycerophosphate acylating fraction in the fat body of Schistocerca gregaria (Forskäl).
pubmed:publicationType
Journal Article