Analytical disk gel electrophoresis with staining techniques for amidohydrolase activity at pH 7.6 demonstrated that partially purified acrosomal extracts of ejaculated bull, boar, and human spermatozoa contained three, apparently four, and two fractions, respectively, with acrosin-like activity. Acrosin amidohydrolase activity is present in the gels incubated in the staining medium at pH 5.0. Some methods for the extraction of human acrosin have been compared. These consist essentially of the extraction by detergent treatment and the extraction by acid procedures. Acid extraction of human spermatozoa yields a higher amount of acrosin than does detergent extraction; the acrosin specific activity, extracted by these methods, seems to be similar.
Multiple forms of boar, bull, and human acrosin / G. Berruti. - In: ARCHIVES OF ANDROLOGY. - ISSN 0148-5016. - 5:3(1980 Nov), pp. 267-277.
Multiple forms of boar, bull, and human acrosin
G. BerrutiPrimo
1980
Abstract
Analytical disk gel electrophoresis with staining techniques for amidohydrolase activity at pH 7.6 demonstrated that partially purified acrosomal extracts of ejaculated bull, boar, and human spermatozoa contained three, apparently four, and two fractions, respectively, with acrosin-like activity. Acrosin amidohydrolase activity is present in the gels incubated in the staining medium at pH 5.0. Some methods for the extraction of human acrosin have been compared. These consist essentially of the extraction by detergent treatment and the extraction by acid procedures. Acid extraction of human spermatozoa yields a higher amount of acrosin than does detergent extraction; the acrosin specific activity, extracted by these methods, seems to be similar.File | Dimensione | Formato | |
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