Abstract
In the crude homogenates of three different strains (C3H, Swiss, C57b) of mouse kidney the exposure to a millimolar concentration of clorgyline reveals a benzylamine oxidative deaminating activity that is due to a clorgyline resistant amine oxidase (CRAO). In the three strains this CRAO activity shows a low sensitivity to semicarbazide and to alpha- amiguanidine. In the C3H mouse kidney the glycoprotein nature of the CRAO was established from affinity chromatography with immobilized concanavalin A. Studies of this activity in the C3H mouse kidney revealed the presence of a reversible inhibitor which is precipitated by ammonium sulphate between 35-55% of saturation. The presence of this inhibitor precludes accurate measurement of the CRAO distribution in the different subcellular fractions. The enzyme purified by affinity chromatography, is semicarbazide insensitive. This is the first observation of the presence of a CRAO-semicarbazide insensitive activity in a tissue. The fact that "original homogenate" and the subcellular fractions show some sensitivity to semicarbazide also indicates that a semicarbazide-sensitive amine oxidase (SSAO) is present in the C3H mouse kidney.
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