The interaction of -chlorohydrin with glycerol kinase

Abstract

.alpha.-Chlorohydrin causes reversible sterility in male rats and several other species. .alpha.-Chlorohydrin was examined for its ability to act as a substrate for glycerol kinase and as an inhibitor of the reaction of glycerol with glycerol kinase. Using a purified enzyme from Candida mycoderma, it was established that .alpha.-chlorohydrin does not act as a substrate for glycerol kinase, but does act as a competitive inhibitor (Ki [inhibition constant] of 30 mM) of purified glycerol kinase and the enzyme present in a sonicated preparation of ram spermatozoa. Neither .alpha.-chlorohydrin nor .alpha.-chlorohydrin phosphate acted as inhibitors of NAD- or flavin-linked glycerolphosphate dehydrogenase. .alpha.-Chlorohydrin apparently does not cause the impairment of sperm metabolism as a result of phosphorylation catalyzed by glycerol kinase.