Abstract
1. 1. Type L pyruvate kinase from normal adult human liver displayed allosteric kinetics towards phospho- enol-pyruvate (PEP), which were enhanced by ATP, citrate, and alanine, and eliminated by fructose-1,6-diphosphate (FDP). 2. 2. Type M pyruvate kinases from human hepatoma and human foetal liver did not show allosteric properties towards phospho- enol-pyruvate and were unaffected by fructose-1,6-diphosphate. 3. 3. ATP and citrate were more potent inhibitors of the L type than of the M type pyruvate kinase, whereas alanine and AMP inhibited the M type enzymes to a slightly greater extent. 4. 4. Alanine inhibition of type M pyruvate kinase was the only one to be relieved by fructose-1,6-diphosphate.
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