Biosynthesis of Acyl Dihydroxyacetone Phosphate in Guinea Pig Liver Mitochondria

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The subcellular distribution of acyl CoA: dihydroxyacetone phosphate acyl transferase in guinea pig liver.

Summarv: Upon differential centrifugation, the enzyme acyl CoA:dihydroxyacetone phosphate acyl transferase (EC 2.3.1.42) in guinea pig liver is shown to sediment in a lysosomal-peroxisomal fraction. Comparison of the distribution of the marker enzymes and of DHAP acyl transferase indicates that the acyl transferase is localized in peroxisomes (microbodies). Acyl dihydroxyacetone phosphate (acyl...

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Purification and properties of acyl/alkyl dihydroxyacetone-phosphate reductase from guinea pig liver peroxisomes.

The peroxisomal acyl/alkyl dihydroxyacetone-phosphate reductase (EC 1.1.1.101) was solubilized and purified 5500-fold from guinea pig liver. The enzyme could be solubilized by detergents only at high ionic strengths in presence of the cosubstrate NADPH. Peroxisomes, isolated from liver by a Nycodenz step density gradient centrifugation, were first treated with 0.2% Triton X-100 to remove the so...

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Glycerolipid biosynthesis in peroxisomes via the acyl dihydroxyacetone phosphate pathway.

In recent years, acyl dihydroxyacetone phosphate [acyl-DHAPt) has been shown to be a precursor of glycerolipids and glycerol-ether lipids.'.' Acyl-DHAP was discovered as a rapidly labeled lipid that was formed in crude mitochondrial fraction from 3'Pi or y-32P[ATP].3 This rapid labeling was due to the enzymatic dephosphorylation and rephosphorylation of endogenous acyl-DHAP present in the crude...

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Biosynthesis of acyl dihydroxyacetone phosphate in subcellular fractions of rat liver.

The activity of acyl-CoA: dihydroxyacetone phosphate acyltransferase in rat liver was studied by measuring the formation of labeled lipid from dihydroxyacetone [W]phosphate and either palmitoyl-CoA or a mixture of palmitate, CoA, and ATP. Bovine serum albumin stimulated the activity of the enzyme several-fold. In the presence of albumin the acyltransferase activity in mitochondria was much high...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1968

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)93330-2