The isolation and characterization of rabbit muscle enolase.

Lohmann and Meyerhof first differentiated, in rabbit muscle extracts, the action of enolase from that of phosphoglyceromutase and pyruvic acid kinase (1). Since that time enolase has been crystallized from yeast by Warburg and Christian (2) and extensively investigated, but the enzyme bearing the same function in muscle tissue has received comparatively little study. A preparation of crystalline muscle enolase by ammonium sulfate fractionation has been reported by Fedorchenko (3), and reference has also been made to Bticher’s unpublished method (4, 5). This paper describes a met’hod for the isolation and crystallization of enolase from rabbit muscle extracts. The molecuIar weight has been estimated from sedimentation and diffusion measurements, and some chemical and biochemical properties of the muscle enzyme have been determined and compared to those of yeast enolase.