Premium
Biochemical characterization of acetyl‐CoA:1‐alkyl‐2‐lyso‐ sn ‐glycero‐3‐phosphocholine acetyltransferase in rat spleen microsomes
Author(s) -
Seyama Kuniaki,
Ishibashi Teruo
Publication year - 1987
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02537300
Subject(s) - phosphocholine , microsome , acetyl coa , clinical chemistry , lipidology , lyso , acetyltransferase , spleen , acetyltransferases , chemistry , biochemistry , enzyme , biology , acetylation , immunology , phospholipid , phosphatidylcholine , scintillator , membrane , detector , electrical engineering , gene , engineering
Abstract Acetyl‐CoA:1‐alkyl‐2‐lyso‐ sn ‐glycero‐3‐phosphocholine (lyso‐PAF) ultrasonic disruption in the presence of 25% glycerol from rat spleen microsomes. About 26% of the enzymatic activity was recovered in the 225,000×g supernatant by this treatment, although the specific activity was slightly decreased compared with the original microsomes. The solubilized enzyme was remarkably susceptible to various kinds of metal ions. Sulfhydryl reagents such as p‐chloromercuribenzoate and N‐ethyl‐maleimide significantly inhibited the enzyme reaction, suggesting that the enzyme is an SH enzyme. Based on the sedimentation pattern in sucrose density centrifugation, the isoelectric point, the kinetic characteristics and the sensitivity to tryptic digestion of microsomes, it appears that acetyl‐CoA:lyso‐PAF acetyltransferase does not differ from the acetyltransferase responsible for the transfer of acetate from acetyl‐CoA to 1‐acyl‐2‐lyso‐ sn ‐glycero‐3‐phosphocholine.