Enzymic synthesis of psychosine sulphate.

Abstract

Abstract—An enzyme which catalyses the synthesis of psychosine sulphate by the transfer of [35S]sulphate from 3′‐phosphoadenosine 5′‐phosphosulphate to galactosyl‐sphingosine has been demonstrated in the brain of the young mouse. The enzyme activity appears to be bound to a microsomal fraction which is spun down with the synaptosomes. The product of the incubation mixture has been characterized as psychosine sulphate by a variety of TLC separations and other chemical procedures. Several parameters (detergent, cations, substrate and 3′‐phosphoadenosine 5′‐phosphosulphate concentrations, pH and incubation time), affecting the 3′‐phosphoadenosine 5′‐phosphosulphate‐psychosine sulphotrans‐ferase activity, have also been investigated. In the normal mouse brain there is a maximum enzyme activity at 17–19 days after birth, which is the period of most rapid myelin formation. In the brains of Jimpy mice, mutants with myelin deficiency, the activity is reduced and reaches a maximum around the 13th day. The lower activity correlates with the small amounts of sulphatides in Jimpy mouse brains. The results are discussed and related to present knowledge of galactolipid biosynthesis.