Abstract
1. 1. The rate of 3-phosphoglycerate exchange with 2,3-diphosphoglycerate catalyzed by phosphoglyceromutase (EC 2.7.5.3) increases in the order, rabbit < yeast < chicken enzymes. 2. 2. Treatment of the chicken and of the rabbit muscle mutase with Hg 2+, a procedure known to increase their 2,3-diphosphoglycerate phosphatase (EC 3.I.3.I3) activity and to decrease their mutase activity, caused 149 and 294% increase, respectively, in their rate of exchange. The phosphate activity of the yeast enzyme which is not affected by Hg 2+ remained also unaffected after Hg 2− treatment in so far as exchange rates between 3-phosphoglycerate and 2,3-diphosphoglycerate. 3. 3. The experimentally observed 32P incorporation from 3-phosphoglycerate into 2,3-diphosphoglycerate was close to that theoretically expected when equilibration of the reaction was reached. 4. 4. The phosphatase activity showed no direct relationship to the rate of the 32P exchange between 3-phosphoglycerate and 2,3-diphosphoglycerate.
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