| Abstract: | The cofactor requirements of brain histidine decarboxylase activity have been studied. Preincubation with carbonyl reagents caused inhibition of the activity ranging from 90% for 10?2m -semicarbazide, 10?3m -phenylhydrazide and 10?3m -hydroxylamine to 50% for isonicotinic acid hydrazide. Sodium borohydride, a reducing agent, also caused complete inhibition of activity. The histidine decarboxylase activity was maximal at 10?4m -pyridoxal-P concentration and was inhibited at higher concentrations of the cofactor. The cofactor-apoenzyme mode of binding was studied by dialysing brain homogenates against several media. Neither the dialysis against buffers alone nor against buffers containing semicarbazide nor cysteine plus EDTA caused a total loss of activity. A 50% of the activity dialysed easily while the other 50% remained ‘tightly’ bound to the apoenzyme. The dialysable and non dialysable activity is evenly distributed between the soluble and particulate activity. |
