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. 1977 Feb;74(2):501–504. doi: 10.1073/pnas.74.2.501

A monomeric form of pyruvate kinase in human pyruvate kinase deficiency.

K Adachi, P K Ghory, T Asakura, E Schwartz
PMCID: PMC392317  PMID: 15247

Abstract

A mutant pyruvate kinase (ATP:pyruvate 2-O-phosphotransferase, EC 2.7.1.40) from human erythrocytes which is easily separated into monomers and dimers by gel chromatography is described. Tht mutant enzyme shows almost the same pH optimum and thermostability as normal enzyme, but has a decreased stability on shaking with air, a decreased Km for phosphoenolpyruvate and a loss of allosteric properties. The apparent Km values for phosphoenolpyruvate of tetramers and monomers were the same. The tetrameric enzyme was slightly activated by fructose-1,6-diphosphate but the monomeric form was not. The tetrameric enzyme was found to dissociate spontaneously to dimeric and monomeric forms.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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