Studies on glycerate 2,3-diphosphatase.

A specific phosphatase for 2,3-diphosphoglyceric acid (2,3DPGA’) has been reported by Rapoport and .Luebering (1) and by Sutherland et al. (2). Rapoport and Luebering (1) studied in some detail a number of the kinetic properties of glycerate2,3+liphosphatase from rat and rabbit skeletal muscle. Wide distribution of this phosphatase in animal tissues has been noted. While in this laboratory, Dr. J. C. Towne found activity for the enzyme in homogenates of beef tissues (heart, brain, muscle, liver, and kidney), and Dr. V. W. Rodwell observed marked activity in water extracts of acetone powders of rabbit brain, heart, and muscle. Rabbit liver and kidney, although active, had lower specific activities (3). This paper presents a method for the purification of glycerate 2,3-diphosphatase from chicken breast muscle and baker’s yeast. A comparative study of the kinetic properties of the enzyme from these two sources is also presented.