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J. Biochem, 1974, Vol. 76, No. 4 847-860
© 1974 Japanese Biochemical Society

research-article

Positional Specificity of sn-Glycerol 3-Phosphate Acylation during Phosphatidate Formation by Rat Liver Microsomes

Yoichi TAMAI* and William E.M. LANDS

Department of Biological Chemistry, The University of Michigan Ann Arbor Michigan, 48104

A microsomal preparation isolated from rat liver catalyzed the acylation of sn-glycerol 3-phosphate with both palmitoyl-CoA and oleoyl-CoA. The optimum pH was 7.5 for both acyl-CoA's, and the apparent Km values for glycerophosphate were 1.0 and 1.2 mM with palmitoyl-CoA and oleoyl-CoA as acyl donors, respectively. The major reaction product was diacyl-sn-glycerol 3-phosphate in the standard assay system with either acyl-CoA.

Acyl-sn-glycerol 3-phosphate (monoacyl-GP) was added to the incubation system to trap newly synthesized radioactive intermediates. Radioactive monoacyl-GP was trapped effectively by the addition of nonlabeled 1-acyl-GP but ineffectively by adding nonlabeled 2-acyl-GP, regardless of whether palmitoyl-CoA or oleoyl-CoA was used as an acyl donor. The monoacyl-GP trapped in the presence of 1-acyl-GP was mostly the 1-acyl-GP isomer, regardless of which acyl-CoA was used. The system with added 2-acyl-GP produced various results as regards the isomeric monoacyl-GP accumulated. Although the pathway via the 2-acyl-GP could not be excluded completely in this experiment, diacyl-GP formation from glycerophosphate in rat liver microsomes appeared to occur primarily via the 1-acyl-GP as an intermediate, regardless of whether palmitoyl-CoA or oleoyl-CoA was used as an acyl donor.

*Present address: Department of Biochemistry, Kitasato University School of Medicine, Sagamihara, Kanagawa.


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