Protein Proteinase Inhibitors in Male Sex Glands

Abstract

Trypsin-specific and trypsin-plasmin inhibitors were isolated from seminal vesicles of guinea pigs. Two different procedures were used: 1. Inhibitor material obtained from perchloric acid extracts was purified by affinity chromatography (using water insoluble trypsin resin) and gradient elution chromatography on Sulfoethyl Sephadex. Mainly two very similar trypsin-specific inhibitors and five somewhat different trypsin-plasmin inhibitors were obtained. (The amino acid compositions are given in Table 3). 2. Also by avoiding the trypsin resin step several inhibitor fractions were obtained which were differing considerably in their amino acid compositions. Inhibitors containing a lysine residue in the reactive site are reversibly inactivated by acylation with maleic anhydride; arginine inhibitors are inactivated by reaction with a butandion-2,3 reagent. In the reactive site of the trypsin-specific inhibitor the sequence Arg-Ile is present. The modified inhibitor (Argile bond is broken) is inactivated by incubation with carboxypeptidase B or reaction with excessive maleic anhydride. The native inhibitor (Arg-Ile bond intact) is converted into the modified form both during contact with the trypsin resin and by incubation with 2.3 mole percent trypsin. From acidic extracts of boar seminal plasma a trypsinplasmin inhibitor was isolated by affinity chromato-This article contains parts of E. FINK, Dissertation,

Localization of Low Molecular Weight Acrosin-Trypsin Inhibitors in the Boar Genital Tract by Immunofluorescence

“…The results of these immunofluorescent studies confirm former observations of Fink et al (1971) showing the production of acid-stable acrosin inhibitors mainly in the seminal vesicles of the boar. The inhibitors are produced and secreted by the epithelium cells of the seminal vesicles.…”

“…tions of various species (Haendle et al -1965;Waldschmidt et al -1966;Fink et al -1971;Zaneveld et al -1971;Suominen and Setchell-1972;.…”

Characterization of mouse epididymal acrosin: comparative studies with acrosin from boar and human ejaculated spermatozoa

“…The inhibitory effect that mouse acrosomal extract has on proacrosin from other species is a strong argument for the existence of a specific acrosin inhibitor in the acrosome of mouse spermatozoa. Several acrosin inhibitors from the epididymal fluid, the seminal plasma and the acrosome, displaying a range of specificities, have been described ( Fink et al ., 1971 ; Polakoski & Williams, 1974; Tschesche et al ., 1982 ; Floerke‐Gerloff et al ., 1984 ; Floerke‐Gerloff et al ., 1985 ). In particular for mouse spermatozoa an intra‐acrosomal acrosin inhibitor, which produces a 3‐fold reduction of the acrosin activity, has already been described ( Bhattacaryya et al ., 1979 ).…”

Intra‐acrosomally located acrosin‐inhibitors: Evolution and developmental patterns in mammals

“…Natural acrosin inhibitors described so far in the literature are components of the seminal plasma that are most probably synthesized in seminal vesicles [Fink et al, 1971;Polakoski and Williams, 1974;Tschesche et al, 19741. These inhibitors exhibit high affinity for both the sperm proteinase acrosin and the secretory proteinase trypsin from the exocrine pancreas [Fritz et al, 19751. In contrast, the two isoinhibitors isolated from crude extracts of ejaculated boar spermatozoa preferentially inactivate acrosin, the K, for the trypsin inhibition being a factor 100 higher than the corresponding K, for acrosin inactivation [Tschesche et al, 19821.…”