Biochemical and histochemical studies on non-specific phosphomonoesterases of swine kidney worm Stephanurus dentatus (Diesing, 1839)
Biochemical and histochemical studies have been made on non-specific acid and alkaline phosphomonoesterases of S. dentatus. The two forms of acid phosphomonoesterases have been found active at pH 4.0 and 6.0. The pH optima for the two forms of aklaline phosphomonoesterases lie at 8.0 and 10.0. Studies on the distribution of acid and alkaline phosphomonoesterases in various tissues have revealed an abundance of acid phosphomonoesterase in various parts of the alimentary canal and various organs of the reproductive system. The excretory ducts show alkaline phosphomonoesterase activity only.
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ABSTRACT: The maximum activity (Vmax) of acid phosphomonoesterase (E.C.220.127.116.11.) at pH 5.5 and 37 degrees C was found to be 2.68 +/- 0.25 and 3.85 +/- 0.24 mu moles phenol mg protein-1 min-1 in male and female Bunostomum trigonocephalum, respectively. The Vmax of alkaline phosphomonoesterase (E.C.18.104.22.168) at pH 10.0 and 37 degrees C was 0.75 +/- 0.04 and 1.15 +/- 0.05 mu moles phenol mg protein-1 min-1 in male and female B. trigonocephalum, respectively. The Michaelis constant (Km) values were 10.25 mM and 11.76 mM for acid and 8.69 mM and 9.09 mM for alkaline phosphomonoesterase in male and female worms, respectively. Enzymal activities were optimum at 7.0 and 9.0% enzyme concentrations, at incubation periods of 60 and 20 min and at temperatures of 50 and 45 degrees C for acid and alkaline phosphomonoesterases, respectively. Dialysis in distilled water decreased the activity of both enzymes, while only acid phosphomonoesterase activity increased in citrate buffer (pH 5.5) and alkaline phosphomonoesterase activity in carbonate buffer (pH 10.0).
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