Some properties of acid and alkaline phosphomonoesterases of chicken spermatozoa.

Abstract:

: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.

journal_name

Andrologia

journal_title

Andrologia

authors

Mohan J,Panda JN,Singh US

subject

Has Abstract

pub_date

1989-01-01 00:00:00

pages

29-34

issue

1

eissn

0303-4569

issn

1439-0272

journal_volume

21

pub_type

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