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Additional resources for Methods of Biochemical Analysis: Analysis of Biogenic Amines and Their Related Enzymes, Supplement Volume
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.