Partial Purification of Cysteine Sulfinic Acid Decarboxylase from Calf Brain.

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Abstract
Cysteinesulfinic acid decarboxylase (EC 4.1.1.29) was purified from calf brain by pH precipitation, ammonium sulfate fractionation, gel filtration and DEAE-Sephadex A-50 chromatography. The enzyme preparation decarboxylated both cysteinesulfinic acid and cysteic acid at all steps of the purification and the ratio of the velocity of decarboxylation of cysteinesulfinic acid to that of cysteic acid was constant, about 2, throughout the purification procedure. The pH optimum was 7.2, both for cysteinesulfinic acid and cysteic acid. The MW of the enzyme was estimated at 65,000 using gel filtration on a Sephadex G-200 column. Its Km was 0.9 mM for cysteinesulfinic acid and 1.6 mM for cysteic acid, with Vmax values of 60.5 and 33.5 nmol/h(mg protein), respectively.