Biochemical characterization of acetyl-CoA:1-alkyl-2-lyso-sn-glycero-3-phosphocholine acetyltransferase in rat spleen microsomes |
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Authors: | Kuniaki Seyama Teruo Ishibashi |
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Affiliation: | (1) Department of Biochemistry, Hokkaido University School of Medicine, 060 Sapporo, Japan |
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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. |
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Keywords: | |
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