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Abstract
Glycolysis has been studied in extracts of rat lens with different concentrations of ATP and AMP as cofactors and various intermediates as substrates.
With optimal concentrations of cofactors, lactate fonnation from glucose approximates that obtained toith equivalent concentrations of pyruvate.
The activity found in extracts is much greater than that observed for the intact lens, so that an enzyme as such is not the limiting factor in lens glycolysis.
With varying cofactor concentrations, steps associated with different enzymes may be limiting. The step associated with hexokinase, 3-phosphoglyceric kinase, or glyceraldehyde phosphate dehydrogenase may be limiting under appropriate circumstances.