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A m . C h m . , 74, 1724 (1952). 60. , and J. GrBgoire, Compt. , I31, 424 (1950). 61. Koerner, J. , and R. L. Sinsheimer, J . Biol. , 228,1039 (1957). 62. Koerner, J. , and R. L. Sinsheimer, J. Biol. , 228, 1049 (1957). 63. Koszalka, T. , R. Falkenheim, and K. I. Altman, Biochzm. et Biophys. 4cta, 23, 647 (1957). 64. Koszalka, T. , S. Horne, B. Schlegel, and K. I. Altman, Biochim. et Biophys. A d a , 36, 197 (1959). 65. , J. , 46, 691 (1955). 66. Kowlessar, 0. , and R. K. McEvoy, J. Clin. , 35, 1325 (1956).

Lems. 100. 0202 4 5 6 7 8 9 PH Fig. 1. Specific RNaae activity in liver fractions at various pH values. mitochondria; 0 = nuclei; x = homogenate; 0 = supernatant fluid; A organic P formed in assay from RNase in mitochondria. From Roth (82). 0 = = in- citrate, NHICl, and urea within a rather wide pH range (24) and, in the case of liver, by a variety of sulfhydryl reagents (85,86). The observation by Holden and Pirie (43) that Cu2+and Fe2+ inhibit pea leaf RNase more at higher pH values led these authors to comment that “the precise position of the optimum will.

U. R. Laurila, and M. Laskowski, J. Biol. , 8SS, 915 ( 1958). 117. , G. Fassina, F. Pochon, and J. Pillet, Bull. 80c. chim. , 40,1905 (1958). 118. Rabatin, J . , R. Friedland, and W. J. Frajola, J. Biol. , 803,23 ( 1953). 119. , and F. Rosuschino, Nuovi ann. , 9, 545 ( 1958). 120. Reichmann, M. , J. Phys. , 6G,831 (1956). 121. , personal communication, 1955. 122. , in E. Chsrgeff and J. N. , The Nucleic Acids, Academic Press, New York, 1955, p. 555. 38 N. B. KURNICK 123. , E. G. Pickels, and P.

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