THE ENZYMATIC ANALYSIS OF SPHINGOMYELIN IN HDL

  • 1 January 1982
    • journal article
    • research article
    • Vol. 20  (5) , 305-312
Abstract
A simple method is described for the enzymatic determination of sphingomyelin in the apolipoprotein B-free supernatants prepared by precipitation of [human] blood sera with phosphotungstate/MgCl2. The analysis is based on the enzymatic hydrolysis of sphingomyelin by sphingomyelinase [EC 3.1.4.12] from Bacillus cereus into phosphorylcholine and N-acylsphingosine, and subsequent hydrolysis of phosphorylcholine by alkaline phosphatase [EC 3.1.3.1]. The choline formed is determined by choline kinase [EC 2.7.1.32] in an optical test. The results from this method were in good agreement with those obtained by the conventional chemical sphingomyelin determination. Furthermore, there was a good correlation between the sphingomyelin concentrations obtained from the HDL [high density lipoprotein] fractions isolated by ultracentrifugation (1.063-1.21 kg/l) and those obtained from the apolipoprotein B free supernatants after phosphotungstate/MgCl2 precipitation of sera.

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