Characteristics of acid phosphatase from rainbow trout (Oncorhynchus mykiss) spermatozoa

Acid phosphatase (AcP) is a commonly observed enzyme in animal semen. In this study, AcP in rainbow trout (Oncorhynchus mykiss) spermatozoa was partly purified and characterized. Extraction in 0.85 percent NaCl with 0.1 percent Triton X-100 enabled obtaining 95 percent of total AcP activity observed...

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Published inArchiwum Rybactwa Polskiego = Archives of Polish Fisheries Vol. 13; no. 2; pp. 131 - 146
Main Authors Sarosiek, B., E-mail: pirosia@pan.olsztyn.pl, Wysocka, J. (Polish Academy of Sciences, Olsztyn (Poland). Inst. of Animal Reproduction and Food Research), Wysocki, P. (University of Warmia and Mazury, Olsztyn (Poland). Dept. of Animal Biochemistry), Glogowski, J. (University of Warmia and Mazury, Olsztyn (Poland). Dept. of Ichthyology)
Format Journal Article
LanguageEnglish
Published Olsztyn Stanislaw Sakowicz Inland Fisheries Institute 01.01.2005
Subjects
acid phosphatase
Actividad enzimática
Activité enzymatique
Analyse enzymatique
Análisis enzimático
Electroforesis
Electrophoresis
Enzimas
Enzymatic analysis
Enzyme
Enzyme activity
Enzymes
Espermatozoo
Freshwater
Oncorhynchus mykiss
Purificación
Purification
Semen
Spermatozoa
Spermatozoïde
Sperme
Électrophorèse
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Summary:Acid phosphatase (AcP) is a commonly observed enzyme in animal semen. In this study, AcP in rainbow trout (Oncorhynchus mykiss) spermatozoa was partly purified and characterized. Extraction in 0.85 percent NaCl with 0.1 percent Triton X-100 enabled obtaining 95 percent of total AcP activity observed in sperm supernatant. Kinetic characteristics were described for the enzyme from sperm extract and for the partly purified enzyme following gel filtration. The optimum pH was 5.8 for unpurified and 5.6 for partly purified enzyme. The affinity of the substrates measured in the sperm extract for p-nitrophenylphosphate dissodium salt and b-glycerophosphate was Km = 1.5 x 10**(-3)M and Km = 1.9 x 10**(-3)M, respectively. The Km for partly purified enzyme was similar at 1.67 x 10**(-3)M measured with p-nitrophenylphosphate dissodium salt. L-tartaric acid and ammonium molybdate were the inhibitors of AcP for unpurified and partly purified enzyme. SDS-PAGE electrophoresis revealed that AcP from rainbow trout had a molecular weight of about 41 kDa
Bibliography:2006000389
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ISSN:1230-6428
2083-6139