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Journal of Lipid Research, Vol 17, 506-515, Copyright © 1976 by Lipid Research, Inc.
BG Rao and MW Spence
A hitherto undescribed sphingomyelinase (sph'ase 7.4) of human brain has
been studied in crude and partially purified (3- to 4- fold) extracts of
grey matter, and compared to the known sphingomyelinase with an acid pH
optimum (sph'ase 5.0). Its specificity for sphingomyelin as substrate is
similar to that of sph'ase 5.0, but it differs from sph'ase 5.0 in its pH
optimum (7.4 vs 5.0) and in a requirement for Mg2+ for optimal activity.
Other properties of sph'ase 7.4 that distinguish it from sph'ase 5.0
include (a) its lack of appreciable solubilization during dialysis of crude
homogenates (b) a more marked concentrations in grey matter than in white
matter (9- to 13- fold vs 1.5- to 2-fold for sph'ase 5.0); (c) inhibition
by Ca2+ and Cd2+ ions, and by EDTA; (D) stimulation by dithiothreitol, and
inhibition by cysteine, N-ethylmaleimide, and p-hydroxymercuribenzoate; (e)
lack of inhibition by nucleotides (AMP.ADP, and ATP) and by NAD plus NADH;
and (f) relative instability to storage or manipulation between -20degrees
C and 40degrees C. These differences indicate the SPH'ASE 7.4 is a
different enzyme protein from sph'ase 5.0. Unlike sph'ase 5.0, which is
widely distributed in mammalian tissues, sph'ase 7.4 occurs predominantly
in grey matter and little activity was observed is spleen, liver, or
leukocytes. The high levels of this enzyme in brain suggest a role related
to the specific functions of this organ or to the need for a more stringent
control of sphingomyelin catabolism in brain as compared to other organs.
ARTICLES
Sphingomyelinase activity at pH 7.4 in human brain and a comparison to activity at pH 5.0
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