Methods of Biochemical Analysis: Analysis of Biogenic Amines

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4) and this elution process was repeated two or three times depending on the yield of the enzyme. The brown eluates were combined (470 ml) and concentrated by precipitation with 120 g of solid ammonium sulfate to 45 % saturation. 4) (Fraction V ) . 4). 4). 0% Triton X-100. Fractions of 14 ml were collected. 3%. The slightly brownish solution was concentrated by pre- 42 H. 4) t o yield Fraclion 1'1. The purified enzyme could be stored in the frozen state. There was an initial loss of 20% in enzyme activity, but after a period of 2 weeks the activity remained constant.

E. Fluorometric Methods for the Determination of M A 0 Activity F. Radiometric Techniques for the Quantitation of M A 0 in Microgram Amounts of Tissue. . . . . . G. Histochemical Demonstration of M A 0 Activity in Various Tissues by the Standard Tryptamine-Tetrazolium Method of Glenner, Burtner, and Brown, Jr. . . . . H. Direct Measurement of M A 0 Inhibition in Humans by the Method of Levine and Sjoerdsma . . . . . 111. Methods of Purification, Crystallization, and Estimation of Histaminase, Diamine Oxidase (DAO) .

0% Triton X-100. Fractions of 14 ml were collected. 3%. The slightly brownish solution was concentrated by pre- 42 H. 4) t o yield Fraclion 1'1. The purified enzyme could be stored in the frozen state. There was an initial loss of 20% in enzyme activity, but after a period of 2 weeks the activity remained constant. Different results were obtained by the authors with different batches of mitochondria. I n about 50% of their experiments the authors obtained enzyme preparations in which the X A O appeared to be solubilized, shown by the fact t hat the enzyme sedimented to the bottom after the addition of ammonium sulfate and, furthermore, th at the enzyme could be dialyzed against buffer which did not contain any detergent.

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