Purification of aldolase C from rat brain and hepatoma.
An isolation procedure for rat brain aldolase C has been developed which also permits the isolation of aldolase C from experimental hepatomas. Certain enzymatic properties (specific activity and Michaelis constant towards the two specific substrates: fructose 1,6-biphosphate and fructose 1-phosphate) and physico-chemical properties (molecular weight, N-terminal amino-acid) of the two enzymes have been studied and compared. Moreover, an amino-acid analysis has been carried out for rat brain aldolase C. Within experimental errors, the two enzymes appear to be identical.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001921:Brain / Q000201:enzymology*; D006528:Carcinoma, Hepatocellular / Q000201:enzymology*; D005634:Fructose-Bisphosphate Aldolase / Q000302:isolation & purification; D005636:Fructosephosphates / Q000378:metabolism; D006801:Humans; D007527:Isoenzymes / Q000302:isolation & purification; D008113:Liver Neoplasms / Q000201:enzymology*; D008970:Molecular Weight; D009374:Neoplasms, Experimental / Q000201:enzymology; D009928:Organ Specificity; D011817:Rabbits; D051381:Rats; D013045:Species Specificity
D000596:Amino Acids; D005636:Fructosephosphates; D007527:Isoenzymes; D005634:Fructose-Bisphosphate Aldolase