Inhibition of glycolysis in boar spermatozoa by alpha-chlorohydrin phosphate appears to be mediated by phosphatase activity.

(R,S)-alpha-chlorohydrin-1-phosphate, previously shown to have no anti-glycolytic activity on mature boar sperm in vitro, is a substrate for acid and/or neutral phosphatase(s) that are associated with washed sperm. The high phosphatase activity hydrolyses the ester to alpha-chlorohydrin which undergoes oxidation to (S)-3-chlorolactaldehyde, a specific inhibitor of sperm glyceraldehyde-3-phosphate dehydrogenase and triosephosphate isomerase, thereby exhibiting an anti-glycolytic action.