Hexokinase has been found in a soluble and a bound form in homogenates of Ascaris suum muscle. Cellulose acetate electrophoresis, isoelectric focusing, and ion exchange chromatography confirmed the presence of only one molecular form of hexokinase in this muscle. A procedure for purifying hexokinase from Ascaris muscle has been developed. The physical and catalytic properties of the enzyme are comparable to mammalian hexokinases. The enzyme is a monomer with a molecular weight of 100,000 as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis and gel filtration. The Michaelis constants for glucose and ATP are 4.7 x 10-3 M and 2.2 x 10-4 M, respectively. Ascaris' hexokinase also exhibits end-product inhibition by glucose 6-phosphate and ADP. It is postulated that the kinetic para meters of the enzyme are the results of its function, that of generating glucose 6-phosphate primarily for glycogen synthesis.

Procedures for the isolation and characterization of Ascaris glyceraldehyde-3-phosphate dehydrogenase and actin are described. The properties of these proteins, including molecular weights, isoelectric points, kinetics, peptide maps, and amino acid compositions, are strikingly similar to the respective proteins from rabbit muscle.

One molecular form of fumarase from Ascaris suum was demonstrated by cellulose acetate electroporesis and isoelectric focusing. The enzyme was partially purified by ammonium sulfate fractionation and ion-exchange chromatography to a specific activity of 49 units per mg protein. Enzymatic assay of the partially purified by ammonium sulfate fractionation amd ion-exchange chromatography to a specific activity of 49 units per mg protein. Enzymatic assay of the partially purified preparation showed glyceraldehyde-3-phosphate dehydrongenase to be the major preparative contaminant.