PMID: 5911524Mar 1, 1966

Enzymic hydrolysis of sphingomyelin by rat liver

The Biochemical Journal
M Heller, B Shapiro

Abstract

1. An enzyme that hydrolyses sphingomyelin to ceramide (N-acylsphingosine) and phosphorylcholine was isolated from rat liver. 2. The enzyme is particle-bound (mitochondria or lysosomes) and can be solubilized by ultrasonic treatment and freezing and thawing. 3. It has been partially purified by precipitation at pH5.2, neutralization and ammonium sulphate fractionation. 4. The enzyme is activated by Triton X-100 (0.2%) or low concentrations of cetyltrimethylammonium bromide (0.02%), higher concentration being inhibitory. 5. The optimum pH is 5-5.5. 6. Of synthetic substrates tested, the erythro isomers of dl-trans-2-N-palmitoyl-1-O-phosphorylcholinesphingosine or dihydrosphingosine were hydrolysed at a rate similar to the natural compound. The threo isomer was hydrolysed much more slowly. The enzyme had little activity on lecithin. 7. The split products of the hydrolysis have little inhibitory effect.

Citations

Apr 15, 1985·European Journal of Biochemistry·J DijkstraG Scherphof
Apr 16, 1973·Biochemical and Biophysical Research Communications·W B WeglickiK Owens
Jan 1, 1972·Acta Pathologica Et Microbiologica Scandinavica. Section B: Microbiology and Immunology·V Lehmann

Related Concepts

Amino Alcohols
Thin Layer Chromatography
Liver
Lysosomes
Mitochondria
Phospholipase
Sphingomyelins

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