. Biological structure and function; proceedings. Biochemistry; Cytology. 244 MAYNARD E. PULLMAN, HARVEY S. PENEFSKY AND E. RACKER for the particulate enzyme of mitochondria and phosphorylating mito- chondrial fragments. Some of these properties are summarized in Table III. While a number of divalent cations including Co + +, Mn + +, Fe + + TABLE III Properties of ATPase Divalent cation required for activity Stimulated by 2,4-dinitrophenol Hydrolyzes ATP, ITP, GTP, and UTP Inhibited by ADP but not IDP Stoicheiometry: ATP + HoO^ADP + Pj Exhibits "latent" activity phenomenon and Ca + +
. Biological structure and function; proceedings. Biochemistry; Cytology. 244 MAYNARD E. PULLMAN, HARVEY S. PENEFSKY AND E. RACKER for the particulate enzyme of mitochondria and phosphorylating mito- chondrial fragments. Some of these properties are summarized in Table III. While a number of divalent cations including Co + +, Mn + +, Fe + + TABLE III Properties of ATPase Divalent cation required for activity Stimulated by 2,4-dinitrophenol Hydrolyzes ATP, ITP, GTP, and UTP Inhibited by ADP but not IDP Stoicheiometry: ATP + HoO^ADP + Pj Exhibits "latent" activity phenomenon and Ca + + substituted for Mg + + in activating the enzyme, only Mg + + and to a lesser extent Co + + gave rise to a dinitrophenol stimulation. The enzyme hydrolyzed ITP, GTP, and UTP in addition to ATP. However, it seems significant that only ATP hydrolysis was stimulated by dinitro- phenol. Neither the nucleoside mono- nor diphosphates were hydrolyzed. O. 0-5 10 1-5 2-0 Preincubation time (hr) 200 Fig. I. Effect of preincubation temperature on ATPase and coupling activity. The purified enzyme was preincubated either at o^ or 30. At the indicated time, aliquots were removed and the appropriate activity measured at 30 as described elsewhere [4]. The specificity of the ADP inhibition is of interest in view of the specificity of this nucleotide in oxidative phosphorylation. The "latent" activity phenomenon referred to in the table may actually be related to the well- known "latent" properties of mitochondrial ATPase [8-10]. It was. Please note that these images are extracted from scanned page images that may have been digitally enhanced for readability - coloration and appearance of these illustrations may not perfectly resemble the original IUB/IUBS International Symposium (1st : 1960 : Stockholm); International Union of Biochemistry; International Union of Biological Sciences; Goodwin, T. W. (Trevor Walworth); Lindberg, Olov, 1914-. London, New York, Academic P
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