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The International journal of biochemistry

Studies on the nature of thiamine pyrophosphate binding and dependency on divalent cations of transketolase from human erythrocytes.


PMID 3248678

Abstract

1. The binding kinetics for [35S]thiamine pyrophosphate to transketolase and the dependency of transketolase on divalent cations for activity were investigated. 2. With Scatchard analysis, dissociation constant (Kd) and n value were calculated to be 0.2 x 10(-6) M and 0.66 respectively. 3. The activity of the reconstituted enzyme increased in the order of Co2+ less than Mn2+ less than Ca2+ less than Mg2+. The native transketolase contained Mg2+ in its molecular structure.

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68138 Transketolase from E. coli, ≥0.1 U/mg