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Zinc inhibits protein phosphorylation in isolated sperm head membranes in Spisula solidissima
Author(s) -
Ahluwalia B.,
Rajguru S.,
Westney L. S.,
Kaul L.
Publication year - 2009
Publication title -
andrologia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.633
H-Index - 59
eISSN - 1439-0272
pISSN - 0303-4569
DOI - 10.1111/j.1439-0272.1991.tb02514.x
Subject(s) - phosphorylation , zinc , sperm , chemistry , phosphatase , protein phosphorylation , divalent , membrane , biochemistry , alkaline phosphatase , dephosphorylation , biology , protein kinase a , enzyme , botany , organic chemistry
Summary. Zinc, when added to the media in concentrations as low as one micromolar, decreased protein phosphorylation in the isolated sperm head membranes in Spisula solidissima , 70–75%. Other divalent cations barium, strontium, cobalt, and copper, in similar concentrations exerted no effect. Sodium fluoride, a phosphatase inhibitor, had no effect on the zinc induced inhibition on protein phosphorylation and, when zinc was added to the media after the phosphorylation reaction of proteins, the inhibitory effect of zinc was lost. The autoradiography of −32 P labeled proteins on SDS gel confirmed the inhibitory effect of zinc on protein phosphorylation. The inhibitory role of zinc on protein phosphorylation in the sperm membranes suggests a physiological role of this cation on membrane activity in the process of fertilization.