. Biological structure and function; proceedings. Biochemistry; Cytology. Fig. 4. Inhibition of DXA formation from CMP by an ATP-regenerating system. Conditions as in Fig. i. Where indicated 4-5 /tmoles of creatine phosphate + o-i mg. of creatine kinase were added. equilibrium between mono-, di- and triphosphates was rapidly established and CDP was the predominating nucleotide. However, when the ATP- regenerating system was added, this resulted in a very efficient phosphoryla- tion of CMP to CTP, and little CDP was left in the system. Since CDP is. Fig. 5. Inhibition of CMP-reduction by an ATP
. Biological structure and function; proceedings. Biochemistry; Cytology. Fig. 4. Inhibition of DXA formation from CMP by an ATP-regenerating system. Conditions as in Fig. i. Where indicated 4-5 /tmoles of creatine phosphate + o-i mg. of creatine kinase were added. equilibrium between mono-, di- and triphosphates was rapidly established and CDP was the predominating nucleotide. However, when the ATP- regenerating system was added, this resulted in a very efficient phosphoryla- tion of CMP to CTP, and little CDP was left in the system. Since CDP is. Fig. 5. Inhibition of CMP-reduction by an ATP-regenerating system. Conditions as in Figs, i and 4. The formation of dCMP + deoxycytidine was measured as described earlier [4]. the substrate for the reduction, the addition of the ATP-regenerating system greatly decreased ribotide reduction. According to this interpreta- tion our experiments indicate that in vitro the synthesis of DNA from ribonucleotides is dependent on the maintenance of a critical level of. 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 Press
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