Phosphatidate synthesis by sn-glycerol-3-phosphate acyl-transferase in pigeon liver particles

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Phosphatidate synthesis by sn-glycerol-3-phosphate acyltransferase in pigeon liver particles.

The properties of acyl-CoA: sn-glycerol-3-phosphate acyltransferase (EC 2.3.1.15) from pigeon liver particles have been studied. The apparent Km for snglycerol 3-phosphate was 50 PM. Acyl-CoA inhibited the enzyme at concentrations exceeding 60 PM. This inhibition can be overcome by adding extra protein. The enzyme was inhibited by thiol-binding agents. Protection from thiol-binding agents is ac...

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Acyl coenzyme A:2-acyl-sn-glycerol-3-phosphate acyltransferase activity in rat liver microsomes.

z-Acylglycerol-3-phosphate can be acylated by acyl-CoA in the presence of microsomal preparations from rat liver. With optimal amounts of substrate, the acyltransferase reaction to the r-position occurred at about one tenth the rate observed for the z-position. Oleate was esterified more rapidly than palmitate or stearate under the conditions used. The enzymic activity catalyzing esterification...

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Characterization of Escherichia coli cells deficient in 1-acyl-sn-glycerol-3- phosphate acyltransferase activity.

A mutant of Escherichia coli K-12 defective in 1-acyl-sn-glycerol-3-phosphate acyltransferase has been isolated. At the permissive temperature for growth, 30 degrees C, 20% of the total cellular glycerophospholipids is 1-acyl-sn-glycerol-3-phosphate, as identified by mass spectral analysis and proton NMR. This percentage of 1-acyl-sn-glycerol-3-phosphate rises to about 30% when the temperature ...

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Acylation of sn-glycerol 3-phosphate by cell fractions of rat liver.

The esterification of sn-glycerol 3-(dihydrogen phosphate) with long-chain fatty acids by rat liver microsomal preparations has been studied. A newly modified spectrophotometric assay for glycerolphosphate acyltransferase (GP-acyltransferase) compared favorably with other assay methods, including measurement of the incorporation of sn-glycerol-(14)C 3-(dihydrogen phosphate) into glycerolipids. ...

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Lipid peroxidation inactivates rat liver microsomal glycerol-3-phosphate acyl transferase. Effect of iron and copper salts and carbon tetrachloride.

Lipid peroxidation is known to affect the activity of several enzymes including microsomal enzymes such as glucose-6-phosphatase; but its effect on the enzymes of lipid biosynthesis has not been investigated. Glycerol-3-phosphate acyltransferase (GPAT) represents the first committed step and probably the rate limiting step in glycerolipid synthesis and thus may be a good candidate for study. Ra...

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ژورنال

عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism

سال: 1970

ISSN: 0005-2760

DOI: 10.1016/0005-2760(70)90224-9