The purification and properties of phosphoglycerate mutase from chicken breast muscle

Abstract

A very rapid procedure for the preparation of phosphoglycerate mutase from chicken breast muscle is presented. Commercially available frozen chicken breasts may be used. The enzyme is obtained in high yields, and the specific activity of the crystalline homogenous preparations is equal to that of the crystalline enzymes from yeast and rabbit muscle. The chicken breast enzyme requires 2,3-diphosphoglycerate for activity, and it is very similar in kinetic and molecular properties to the rabbit muscle phosphoglycerate mutase. Similarly, it also possesses 4 sulfhydryl groups per mole of enzyme. The molecular weight of the enzyme is 65,690. With the use of a gel filtration technique, it has been demonstrated that 2 moles of 2,3-diphosphoglycerate may be bound per mole of the enzyme. It appears that the binding of this phosphoglycerate may entail phosphoenzyme formation. Again, as with other pure phosphoglycerate mutases, the chicken breast muscle mutase shows some 2,3 phosphoglycerate phosphatase activity (about l/40,000 the mutase activity).