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Some Properties of Acid and Alkaline Phosphomonoesterases of Chicken Spermatozoa/Eigenschaften der suaren und alkalischen Phosphomonesterase von Hühnerspermatozoen

Summary: Alkaline (ALP) and acid (ACP) phosphomonoesterases present in the cell‐free extracts of the Triton x‐100 treated freshly ejaculated chicken spermatozoa were studied of some of their physico‐chemical properties. Alkaline Phosphomonoesterase was found to have the optimal specific activity at pH 7.6 in 100 mM Tris‐HCl buffer and was temperature‐dependent and reached its peak at 70 °C. This activity was stimulated by Mn++, Co++, Mg++ and Fe++ ions and inhibited by Cu++, Hg++, Ca++, EDTA and dithiothreitol. Acid phosphomonoesterase, in similar conditions of assay procedure, had optimal activity at pH 5.0 at 60 °C after 30 min incubation. It was stimulated by Co++, Mg++, EDTA and dithiothereitol, but other divalent ions and N‐ethylmaleimide inhibited the activity. These data suggest that these enzymes of chicken spermatozoa are some how different in character from those of mammalian ones.