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Binding of 2,3-Diphosphoglycerate (DPG) to Oxyhemoglobin; Levels and Effect of DPG on Oxygen Affinity of Normal and Abnormal Blood

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Red Cell Metabolism and Function

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 6))

Abstract

My awareness of 2,3-diphosphoglycerate (DPG) started over 20 years ago when I occupied a bench in a laboratory shared by my teacher Ochoa with Greenwald, who had some 20 years earlier discovered DPG in the red cell (1). Nevertheless, my interest in DPG came about in a round about way. In the late 40’s was demonstrated for the first time the use of ATP, at the enzyme level, for synthetic reactions, i.e., urea and glutamine synthesis (2). At the suggestion of Ochoa, Ratner and then I started to use 3 PGA in a generating system for ATP; a technique which, by the way, became so popular that possibly it has been forgotten, if ever recognized, that it originated with Ochoa. The need of a glycolytic system free from interfering phosphatases led me to purify phosphoglyceromutase, which up to then had been studied only in crude preparations. Possibly a misfortune was the fact that Rodwell, then one of my students was lucky in crystallizing the enzyme for the first time; since that time I have been most reluctant to lose interest in the phosphoglycerate area. Of course today with the advances in enzymology, it is only a matter of patience to achieve enzyme crystallization as pointed out recently by Theorell (3).

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Grisolia, S., Carreras, J., Diederich, D., Charache, S. (1970). Binding of 2,3-Diphosphoglycerate (DPG) to Oxyhemoglobin; Levels and Effect of DPG on Oxygen Affinity of Normal and Abnormal Blood. In: Brewer, G.J. (eds) Red Cell Metabolism and Function. Advances in Experimental Medicine and Biology, vol 6. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3195-7_4

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