Journal of Lipid Research, Vol. 7, 379-386, May 1966
Copyright © 1966 by Lipid Research, Inc.

Cerebroside galactosidase of brain

Amiya K. Hajra , David M. Bowen , Yasuo Kishimoto , and Norman S. Radin

Mental Health Research Institute, University of Michigan, Ann Arbor, Michigan

The galactoside bond in cerebroside was found to be cleaved by an enzyme in rat and pig brain. Emulsified stearoyl-¹⁴C psychosine was used as the substrate and the extent of cleavage was studied by isolating and counting the stearoyl sphingosine (ceramide) formed. The reaction products, ceramide and galactose, were characterized by column and thin-layer chromatography. Cerebroside containing galactose-³H was also used to show liberation of galactose. Cholic acid was found to be required for activation of the enzyme, which has a pH optimum of 4.5. Similar cerebrosidase activity was found in spleen, kidney, and lung of rat; liver and heart showed very slight activity.

The partially purified enzyme from pig brain also formed ceramide from ceramide lactoside, ceramide glucoside, and cerebronoyl psychosine. The enzyme was active toward o-nitrophenyl galactoside and could be fractionated by Sephadex chromatography into a fraction active toward the nitrophenyl galactoside only and a fraction active toward both this substrate and ceramide galactoside. Human spleen, normal and Gaucher, exhibited cerebrosidase activity.

Supplementary key words stearoyl-¹⁴C psychosine • cerebronoyl-¹⁴C psychosine • cerebrosidase • rat organs • pig brain • ceramide • ceramide lactoside • galactosidase • ceramide • glucoside • Gaucher spleen • glucosidase

Submitted on July 6, 1965
Revised on December 30, 1965
Accepted on January 20, 1966

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