Hoppe-Seyler's Z. Physiol. Chem. . 357, S. 855 - 865, Juni 1976 Multiple Forms of Human Acrosin: Isolation and Properties Wolf-Dieter SCHLEUNING, Ruza HELL and Hans FRITZ Institut für Klinische Chemie und Klinische Biochemie der Universität München (Received 26 February 1976) Summary: Human acrosin was purified to electrophoretically homogeneous forms by acidic extraction of washed ejaculated spermatozoa and gel filtration of the acidic extracts on Sephadex G-75, followed by affinity chromatography onp-aminobenzamidine Sepharose. Human acrosin exists in at least four molecular forms. The apparent molecular weights of three forms were determined to be 64000, 38000 and 25000, respectively. The high molecular weight form is transformed to the low molecular weight forms by incubation of the acrosin preparation obtained from freshly ejaculated spermatozoa in solutions of pH near 7. Like boar acrosin, human acrosin is also a glycoprotein and therefore reversibly bound to Concanavalin A-Sepharose. The amino acid composition of the 25 000 molecular weight form is similar to that of human trypsin. Rabbit anti-boaracrosin -globulins form a precipitate with human acrosin, but not with porcine trypsin or human plasmin. The relationship between the occurrence of multiple acrosin forms and proenzyme activation by limited proteolysis is discussed. Verschiedene Formen
hoppe-seyler's zeitschrift für physiologische chemie – de Gruyter
Published: Jan 1, 1976
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