The synthesis of higher glycerides via the monoglyceride pathway in hamster adipose tissue

Schultz, F. Michael; Johnston, John M.

doi:10.1016/s0022-2275(20)39521-3

Cited by 47 publications

(1 citation statement)

References 29 publications

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“…For the largest experiment (six animals) the significance levels were P<0.01 for 2-palmitoylglycerol and rac-l-monopalmitoylglycerol, and P< 0.001 for 2-monopalmitoylglycerol and 2-hexadecylglycerol. Schultz & Johnston (1971) have reported on the difficulties of interpreting results obtained with 2-monoacylglycerols which probably results from the rapid hydrolysis and isomerization of this substrate.…”

Section: Discussionmentioning

confidence: 99%

A new assay procedure for monoglyceride acyltransferase

Short

Brindley

Dils

1974

Biochemical Journal

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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.

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Section: Discussionmentioning

confidence: 99%