Abstract
Publisher Summary Dihydroxyacetone phosphate acyltransferase (DHAPAT) catalyzes the transfer of the fatty acid moiety from long-chain acyl-coenzyme A (acyl-CoA) to the free hydroxyl group of dihydroxyacetone phosphate. This reaction initiates the synthesis of the ether-linked glycerolipids and the more common glycerol ester lipids. DHAPAT is an integral membrane-bound protein located on the luminal side of animal cell peroxisomes. Its enzyme activity is measured as the amount of lipophilic (at low pH) radioactivity formed from [ 32 P]DHAP in the presence of palmitoyl-CoA and enzyme. The purification of DHAPAT can be divided into three processes: (1) isolation of peroxisomes, (2) solubilization of the peroxisomal membranes, and (3) chromatographic purification of DHAPAT. The solubilized DHAPAT is purified to near homogeneity by a multistep regimen of both low-pressure and high-pressure column chromatography. A number of genetic diseases involving peroxisomal disorders are prenatally or postnatally diagnosed by the decreased activity of DHAPAT in aminocytes, chorionic villi, leukocytes, or in cultured skin fibroblasts obtained from the patients.
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