Activation of an erythrocyte NAD:arginine ADP-ribosyltransferase by lysolecithin and nonionic and zwitterionic detergents

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Abstract
The activity of an NAD:arginine ADP-ribosyl-transferase was stimulated 4- to 6-fold by lysolecithin; lysolecithins containing long-chain fatty acids such as stearoyl (C18) and palmitoyl (C16) were more effective than those with shorter chains: C14 > C12 > C10 .simeq. C8. The analog lacking a fatty acid at C-1, .alpha.-glycerophosphocholine, was inactive as were choline, lysophosphatidic acid, lysophosphatidylserine, lysophosphatidylglycerol, lysophosphatidylethanolamine, lecithin, phosphatidic acid, phosphatidylserine and phosphatidylethanolamine. Activation of the transferase was, however, also observed with certain nonionic (e.g., Triton X-100) and zwitterionic [3-[(cholamidopropyl)dimethylammonio]-1-propanesulfonate] detergents. The transferase was shown previously to be stimulated by chaotropic salts or histones; in the presence of maximally effective concentrations of lysolecithin, salt, and histone, the activity was similar to that observed in the presence of histone or salt alone. Maximal activation by lysolecithin and detergents was less than that observed with either salt or histone. Activation by lysolecithin shows significant differences from that observed previously with histones or salt and can be mimicked by certain nonionic and zwitterionic detergents.

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