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Kinetic Mechanism of Allosteric Regulation of Muscle Glycogen Phosphorylase b by Adenosine 5"-Monophosphate

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Abstract

Kinetic analysis of the glycogen chain growth reaction catalyzed by glycogen phosphorylase b from rabbit skeletal muscle has been carried out over a wide range of AMP concentration under the saturation of the enzyme by glycogen. Applicability of some variants of the kinetic model involving the interaction of AMP- and glucose 1-phosphate-binding sites in the dimeric enzyme molecule is considered. A kinetic model of the enzymatic reaction describing adequately the activation of the enzyme by AMP and inhibition at sufficiently high concentrations of AMP is proposed.

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  1. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, Moscow, 117071, Russia

    S. V. Klinov & B. I. Kurganov

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  1. S. V. Klinov
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  2. B. I. Kurganov
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Klinov, S.V., Kurganov, B.I. Kinetic Mechanism of Allosteric Regulation of Muscle Glycogen Phosphorylase b by Adenosine 5"-Monophosphate. Biochemistry (Moscow) 66, 1374–1377 (2001). https://doi.org/10.1023/A:1013385813266

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