Abstract

An h.p.i.c.-based assay for cysteinesulphinic acid decarboxylase has been developed. The assay simultaneously measures glutamate decarboxylation and/or taurine formation. Using the cysteinesulphinic acid decarboxylase in rat liver homogenate, L-[2-2H1]cysteinesulphinic acid was converted into [2-2H1]hypotaurine. Similarly, unlabelled L-cysteinesulphinic acid was transformed by rat liver homogenate in a D2O-containing medium into the enantiomeric [2-2H1] hypotaurine. The products were desulphurized by treatment with Raney nickel, and the resulting enantiomeric [1-2H1]ethylamines converted into the corresponding (–)-camphanamides. Deuterium n.m.r. spectra of the latter revealed that the decarboxylations proceeded stereospecifically with retention of configuration.

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