PURIFICATION AND SOME PROPERTIES OF PYRUVATE-KINASE FROM THE SKELETAL-MUSCLE OF AFRICAN LAND TORTOISE KINIXYS-EROSA (LINN)

1. Pyruvate kinase from Africa land tortoise (Kinixys erosa) skeletal muscle was isolated and purified to homogeneity. 2. The mol. wt of the enzyme was estimated to be 212,333 +/- 2887 with four subunits of 49,680 +/- 526. 3. The enzyme, denatured by 4M guanidine-HCl, regained a maximum of 80-87% of its original activity upon dilution at 20-degrees-C and at a protein concentration of 80-mu-g/ml in appropriate buffer containing 10 mM PEP and 1 mM L-valine. The kinetics of renaturation was first order. 4. The catalytically active renatured enzyme was a dimer even though it was kinetically similar to the tetrameric native enzyme.