Some properties of acid and alkaline phosphomonoesterases of chicken spermatozoa.
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 degrees 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 degrees 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.
Mohan
J
J
Division of Physiology & Reproduction Central Avian Research Institute, India.
Panda
J N
JN
Singh
U S
US
D000818:Animals; D002413:Cations, Divalent; D002645:Chickens / Q000378:metabolism*; D004789:Enzyme Activation; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D008297:Male; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D013094:Spermatozoa / Q000201:enzymology*
D002413:Cations, Divalent; D010744:Phosphoric Monoester Hydrolases