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Am J Physiol Cell Physiol 257: C29-C35, 1989;
0363-6143/89 $5.00
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AJP - Cell Physiology, Vol 257, Issue 1 C29-C35, Copyright © 1989 by American Physiological Society

ARTICLES

Binding of adenylosuccinate synthetase to contractile proteins of muscle

J. P. Manfredi, R. Marquetant, A. D. Magid and E. W. Holmes
Department of Medicine, Duke University, Durham, North Carolina 27710.

The muscle isozyme of adenylosuccinate synthetase (AdSS), an enzyme of the purine nucleotide cycle, has previously been shown to bind to purified F-actin in buffers of low ionic strength and pH (Ogawa et al. Eur. J. Biochem. 85: 331-338, 1978). We have extended these observations by measuring the association of both crude and purified AdSS with the contractile proteins of muscle in buffers of physiological ionic strength and pH. Under these conditions, the enzyme binds to F-actin, actin-tropomyosin complexes, reconstructed thin filaments, and myofibrils but not to myosin. The apparent dissociation constant of 1.2 microM and binding maximum of 2.6 nmol enzyme/mg myofibrils indicate that binding of AdSS to myofibrils can be physiologically significant. The results suggest that AdSS in muscle may be associated with the thin filament of myofibrils.


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