Linked Life Data

6653926

Source:http://linkedlifedata.com/resource/pubmed/id/6653926

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1984-2-14
pubmed:abstractText
Acyl-CoA: monoglyceride acyltransferase (MGAT; EC 2.3.1.22) has been studied in human small intestinal mucosa by means of a spectrophotometric method based on the detection of liberated CoA employing 5,5'-dithiobis-(2-nitrobenzoic acid). With optimal assay conditions available the pH optimum was spread between 7.0 and 7.7 with a maximum at a pH of 7.4. Dependent on its concentration one of the substrates, palmitoyl-CoA, caused severe inhibition which was largely prevented by the addition of albumin. Using palmitoyl-CoA and 1-monooleoylglycerol as substrates specific activities were 23.0 +/- 8.4 in total homogenates compared with 92.9 +/- 28.3 nmol CoA released/min/mg protein in microsomal fractions from jejunal mucosa. Concerning the substrate specificity, a broad acyl-donor pattern exists with maximal activities for C10:0 to C16:0, the highest for C16:0. A preferential esterification of acyl-acceptors was shown for 2-monoacylglycerols as compared with the 1-isomers, and for monoacylglycerols with unsaturated versus saturated fatty acids. MGAT was mainly localized in the microsomal fraction. The properties of MGAT from human small intestine are discussed with respect to the intestinal enzyme from other species.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0012-2823
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
138-47
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Triacylglycerol biosynthesis in human small intestinal mucosa. Acyl-CoA: monoglyceride acyltransferase.
pubmed:publicationType
Journal Article