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Transketolase variant enzymes and brain damage.

O E Pratt, M Jeyasingham, G K Shaw

    Alcohol and Alcoholism (Oxford, Oxfordshire)
    |January 1, 1985
    PubMed
    Summary

    Human red blood cell transketolase exists in two forms: one with bound thiamine diphosphate and a smaller, low-affinity variant. Clinical tests may mask activation due to excess thiamine diphosphate inhibiting the high-affinity form.

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    Area of Science:

    • Biochemistry
    • Enzymology

    Background:

    • Human red blood cell transketolase is crucial for cellular metabolism.
    • The enzyme's activity is dependent on its coenzyme, thiamine diphosphate.
    • Clinical assessments of transketolase activation are commonly used.

    Purpose of the Study:

    • To investigate the heterogeneity of human red blood cell transketolase.
    • To understand the interaction of enzyme variants with thiamine diphosphate.
    • To explain discrepancies in clinical transketolase activation tests.

    Main Methods:

    • Gel filtration to resolve transketolase into components.
    • Analysis of enzyme activity with varying thiamine diphosphate concentrations.
    • Separation and characterization of enzyme variants.

    Main Results:

    • Transketolase resolved into two components: high-affinity (firmly bound coenzyme) and low-affinity (smaller molecule).
    • Low-affinity variant requires added thiamine diphosphate and shows reduced affinity.
    • Excess thiamine diphosphate inhibits the high-affinity form, masking low-affinity variant activation in normal hemolysates.

    Conclusions:

    • Human red blood cell transketolase exists in at least two variants, including a low molecular weight, potentially damaged form.
    • Abnormal conditions like alcoholism and thiamine deficiency may increase the proportion of the low molecular weight variant.
    • A modified mechanism for transketolase's role in thiamine deficiency-related brain damage is proposed.

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