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• W1566018690 abstract "Five acid phosphatases, S4, S3, S2, Szn and S1 (orthophosphoric monoester phosphohydrolase, EC 3.1.3.2) of ejaculated rabbit spermatozoa were either partially purified by DEAE-Sephadex column chromatography or prepared by specific extraction methods. The pH optimum of S4 was 6.0–6.5 in acetate buffer and 7.0 in Tris-HCl buffer; the pH optima of S3, S2, Szn, and S1 were 4.5, 5.5., 6.0 and 5.2, respectively, in acetate buffer. The apparent molecular weights of S3, S, Szn and S1, determined by disc gel electrophoresis, were 123 000, 86 000, 64 000 and 45 000–49 000, respectively. Incubation with neuraminidase did not alter the electrophoretic mobilities of any of the enzymes. Ten natural phosphoric esters were tested as substrates. S4 preferentially hydrolyzed ATP, ADP, PPi and 3′-AMP. S3 hydrolyzed only β-glycerophosphate and glucose 6-phosphate to a significant extent. S2 hydrolyzed β-glycerophosphate, glucose 1-phosphate, the phosphoproteins, casein and phosvitin. S1 hydrolyzed ADP and β-glycerophosphate most readily. Szn may be an ATPase since it exhibits very high Zn2+-stimulated against ATP. These characteristics combined with the effects of NaF, ZnCl2, l-(+)-tartaric acid, and formaldehyde on the activity of each partially purified enzyme with α-naphthyl phosphate as substrate indicate that these phosphatases are structurally and functionally different." @default.
• W1566018690 created "2016-06-24" @default.
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• W1566018690 date "1973-08-01" @default.
• W1566018690 modified "2023-09-24" @default.
• W1566018690 title "Acid phosphatases of rabbit spermatozoa" @default.
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• W1566018690 doi "https://doi.org/10.1016/0304-4165(73)90177-3" @default.
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