Interaction of glyceraldehyde-3-phosphate dehydrogenase with isolated microsomal subfractions of skeletal muscle.

Twinning in crystals of human skeletal muscle D-glyceraldehyde-3-phosphate dehydrogenase.

Glycolytic enzymes in different types of skeletal muscle: adaptation to exercise.

BALDWN, K. M., W. W. WINDER, R. L. TERJUNG, AND J. 0. HOLLOSZY. Glycoi’ytic enzymes in di$erent types of skeletal muscle: adaptation to exercise. Am. J. Physiol. 225(4): 962-966. 1973.-The level of activity of hexokinase increased 1700/;, in red skeletal muscle (red portion of quadriceps), 50y0 in intermediate (soleus), and 30% in white skeletal muscle (white portion of quadriceps) in rats subj...

Identification of an arginine residue important for catalytic activity in the primary structure of D-glyceraldehyde 3-phosphate dehydrogenase. Studies with the rat skeletal-muscle enzyme.

The reaction of holo-(D-glyceraldehyde 3-phosphate dehydrogenase) (EC 1.2.1.12) from rat skeletal muscle with [14C]butanedione in 0.05 M-NH4HCO3, pH 8.0, resulted in modification (*) of two arginine residues per subunit with a concomitant loss of catalytic activity. From a tryptic digest of the modified protein two radiolabelled peptides were isolated, with the following sequences: (1)Val-Ile-I...

Fluorescence studies on glyceraldehyde-3-phosphate dehydrogenase from bovine heart muscle.

Glyceraldehyde-3-phosphate dehydrogenase is a glycolytic enzyme that catalyses conversion of glyceraldehyde-3-phosphate to 1,3-diphosphoglycerate. ATP has been found to have an inhibitory effect on this enzyme. To establish the interaction between the enzyme and ATP, a fluorescence technique was used. Fluorescence quenching in the presence of ATP suggests cooperative binding of ATP to the enzym...

Purification and properties of glyceraldehyde-3-phosphate dehydrogenase from the skeletal muscle of the hibernating ground squirrel, Ictidomys tridecemlineatus

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from the skeletal muscle of euthermic and torpid Ictidomys tridecemlineatus was purified to electrophoretic homogeneity using a novel method involving Blue-agarose and Phenyl-agarose chromatography. Kinetic analysis of the enzymes isolated from the two conditions suggested the existence of two structurally distinct proteins, with GAPDH V max bein...