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

Authors
  • Moss, J
  • Osborne, J C Jr
  • Stanley, S J
Type
Published Article
Journal
Biochemistry
Publication Date
Mar 27, 1984
Volume
23
Issue
7
Pages
1353–1357
Identifiers
PMID: 6426504
Source
Medline
License
Unknown

Abstract

The activity of an NAD:arginine ADP-ribosyltransferase was stimulated 4-6-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 greater than C12 greater than C10 congruent to C8. The analogue 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. It appears that 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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