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Measurements of the alkali cation content of spermatozoa from several mammals (Quinn & White, 1967, 1968a; O'Donnell, 1969) suggested that these cells may possess active transport systems for sodium and potassium, and an ATPase with the properties of an alkali cation-transport system has been demonstrated in the spermatozoa of bull, boar and ram (Quinn & White, 1968b) located mainly in the mid-piece. The cardiac glycosides, ouabain and digoxin, which specifically bind to ATPase sites on the membranes of a variety of mammalian cells (Matsui & Schwartz, 1968; Ellory & Keynes, 1969; Baker & Willis, 1969), have been shown to bind to the cell membrane of the mid-piece—tail region in bull spermatozoa (O'Donnell & Ellory, 1970). Although the binding occurred at a membrane site in proximity to a source of metabolic energy and was sensitive to metabolic inhibition, the binding
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