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In order to elucidate the nature of the binding of cadmium to rat testis a detailed study of the isolation and characterization of cadmium-binding protein from this organ was undertaken. Cadmium-109 was injected intraperitoneally into rats which were killed after 24 hr. The protein labelled with cadmium-109 was isolated using Sephadex gel filtration with G-75 and G-25. The cadmium bound selectively in vivo to a low molecular weight protein and cadmium-109 remained bound to the cadmium-binding protein at pH 7 but dissociated from it at pH 2. The ultraviolet absorption spectra were characteristically different at the 2 pH values. The molecular weight of the protein was 15000 as determined by Sephadex G-75 gel filtration. Disc-gel electrophoresis showed 1 major and 2 minor bands. All these observations suggest that rat testis cadmium-binding protein though similar in some respects differs from cadmium-binding protein of liver and kidney in absorption spectra molecular weight and disc-gel electrophoresis.

ISOLATION AND CHARACTERIZATION OF CADMIUM-BINDING PROTEIN FROM RAT TESTES