NDLI: A new assay procedure for monoglyceride acyltransferase.

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A new assay procedure for monoglyceride acyltransferase.

Content Provider	Semantic Scholar
Author	Short, V. J. Brindley, David N. Dils, R. R.
Copyright Year	1974
Abstract	1. A new assay system is described for monoglyceride acyltransferase (acylglycerol palmitoyltransferase, EC 2.3.1.22) in which palmitoyl-CoA is generated from palmitoyl-(-)-carnitine. 2. With the microsomal fraction from homogenates of guinea-pig intestinal mucosa, the V(max.) of this enzyme decreased with different acyl acceptors in the order 2-monopalmitoylglycerol>2-hexadecylglycerol>rac-1-monopalmitoylglycerol. 3. There were highly significant correlations between the monoglyceride acyltransferase activity as measured with these three substrates. This demonstrates that each of these substrates can be used to measure the same enzyme activity. 4. The advantages of using generated palmitoyl-CoA with 2-hexadecylglycerol and rac-1-monopalmitoylglycerol as model substrates for this enzyme are discussed.
Starting Page	1
Ending Page	6
Page Count	6
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.biochemj.org/content/ppbiochemj/141/2/407.full.pdf
PubMed reference number	4455214v1
Volume Number	141
Issue Number	2
Journal	The Biochemical journal
Language	English
Access Restriction	Open
Subject Keyword	2-acylglycerol O-acyltransferase Acylglycerol Acyltransferase Carnitine O-Palmitoyltransferase Intestinal Mucosa Monoglycerides Palmitoyl-CoA Hydrolase enzyme activity
Content Type	Text
Resource Type	Article

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