Fatty acid activation and temperature perturbation of rat brain microsomal phospholipase D.
The hydrolytic and transphosphatidylation activities of rat brain microsomal phospholipase D were highly latent in the absence of an appropriate activator. The most suitable surfactants for this activation were oleate and palmitoleate. Besides the bile acids and unsaturated fatty acids, other naturally occurring surfactants, such as lysophospholipids, acidic phospholipids, acyl-CoA's, and gangliosides, were inactive. Taurodeoxycholate, at optimal concentration, produced a profound inhibition of oleate activation. Phospholipase D activity was detectable in all rat tissues investigated. The optimal incubation temperature for phospholipase D was 30 degrees C, with a break point at 16.1 degrees C in an Arrhenius plot.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D004789:Enzyme Activation / Q000187:drug effects; D005227:Fatty Acids / Q000494:pharmacology*; D008861:Microsomes / Q000201:enzymology*; D019301:Oleic Acid; D009829:Oleic Acids / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000494:pharmacology; D010739:Phospholipase D / Q000378:metabolism*; D010740:Phospholipases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D013657:Taurodeoxycholic Acid / Q000494:pharmacology; D013696:Temperature
D005227:Fatty Acids; D009829:Oleic Acids; D019301:Oleic Acid; C013173:osteum; D013657:Taurodeoxycholic Acid; D010740:Phospholipases; D010739:Phospholipase D; D010447:Peptide Hydrolases