Ital J Biochem
December 1983
Diamide, directly added to human erythrocytes, inhibits glucose utilisation. The trend of this process is in good correlation with the intracellular concentration of GSH. Since diamide does not affect the glycolytic and hexose monophosphate-shunt-pathway enzymes, it is likely that the effect of diamide involves the sugar transport across erythrocyte membrane.
View Article and Find Full Text PDFReaction of rabbit muscle fructose 1,6-P2 aldolase with methylglyoxal results in a biphasic loss of activity. The kinetics of the initial rapid phase are first order with respect to the inhibitor. Dihydroxyacetone phosphate and fructose 1,6 bisphosphate afford complete protection whereas inorganic phosphate provides only a partial protection against inactivation.
View Article and Find Full Text PDFFructose 1,6-bisphosphate aldolase inactivation by L- and D-glyceraldehyde 3-phosphate (Ga 3-P) obeys pseudo first-order kinetics. L-Ga 3-P is much more effective than the D-isomer: the Ki values obtained are 0.032 mM and 0.
View Article and Find Full Text PDFThe platelets function of newborn aroused great interest in these last years. On this line, AA. made the stretching test according to Breddin K.
View Article and Find Full Text PDFSelenalysine is more effective than lysine both on glyceraldehyde 3-P transformation into methylglyoxal and on subsequent methylglyoxal polymerization.
View Article and Find Full Text PDFItal J Biochem
September 1977
L(+)--lysine reacts with methylglyoxal in aqueous solution to give a yellow polymer. This polymer has been subjected to some chemical and physico-chemical characterizations. The gross structure of the polymer is probably formed by 3-hydroxypyrrolic nuclei, bridged together by vinylenic groups or -CH(OH)-CH2-CO-CH(OH)-groups.
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