Pentose phosphate metabolizing enzyme activity of leukocytes in patients of various age groups.
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The NADP-dependent glycerol-3-phosphate dehydrogenase activity in liver, heart and skeletal muscle of rat was studied. The activity is found when glyceraldehyde-3-phosphate or ribose-5-phosphate in the presence of ATP are taken as substrates. The data obtained confirm that NADP-dependent glycerol-3-phosphate dehydrogenase exists in skeletal muscle and demonstrate that it is found in heart muscle as well.
In a supernatant of rat kidney cortex homogenate activities of glucose-6-phosphate and 6-phosphogluconate dehydrogenases were shown to be approximately equal. These enzymes were found in kidney medulla; their activities, similar to those glycolytic enzymes, were higher in kidney medulla than in cortex. In diabetes the activity of glucose-6-phosphate dehydrogenase from kidney cortex was increased.
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Hydroxythiamin was shown to inhibite distinctly phosphofructokinase and phosphohexoisomerase besides a direct antivitaminous effect on transketolase. In this case the regulatory action is likely to be carried out by erythrose-4-phosphate, accumulating in liver tissue. Citrate (administered separately and together with hydroxythiamin) is assumed to influence indirectly the transketolase activity affecting the total regulation of carbohydrate metabolism.