Interaction of Phosphorylase Kinase from Rabbit Skeletal Muscle with Flavin Adenine Dinucleotide

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V. F. Makeeva^*, N. A. Chebotareva, I. E. Andreeva, N. B. Livanova, and B. I. Kurganov

Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, 119071 Moscow, Russia; fax: (495) 954-2732; E-mail: makeeva@inbi.ras.ru

^* To whom correspondence should be addressed.

Received August 18, 2005; Revision received September 21, 2005

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The interaction of flavin adenine dinucleotide (FAD) with rabbit skeletal muscle phosphorylase kinase has been studied. Direct evidence of binding of phosphorylase kinase with FAD has been obtained using analytical ultracentrifugation. It has been shown that FAD prevents the formation of the enzyme-glycogen complex, but exerts practically no effect on the phosphorylase kinase activity. The dependence of the relative rate of phosphorylase kinase-glycogen complex formation on the concentration of FAD has cooperative character (the Hill coefficient is 1.3). Under crowding conditions in the presence of 1 M trimethylamine-N-oxide (TMAO), FAD has an inhibitory effect on self-association of phosphorylase kinase. The data suggest that the complex of glycogen metabolism enzymes in protein-glycogen particles may function as a flavin depot in skeletal muscle.

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KEY WORDS: phosphorylase kinase, FAD, glycogen, trimethylamine-N-oxide, turbidimetry, sedimentation, association

DOI: 10.1134/S0006297906060095

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