Effect of mild heat treatment on action and nucleotide binding of myosin subfragment 1

Chymotryptic subfragment 1 (S-1) prepared from rabbit skeletal myosin has lost its ATPase activity upon incubation at 35 degree C for 3 h. The loss in ATPase activity was accompanied by the perturbation of the structure of the 50K domain as indicated by a dramatic increase in the tryptic susceptibil...

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Bibliographic Details
Published in:Biochemistry (Easton) 1988-01, Vol.27 (2), p.792-796
Main Authors: Setton, A, Dan-Goor, M, Muhlrad, A
Format: Article
Language:English
Subjects:
myosin
mysin ATPase
rabbits
skeletal muscle
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Summary:Chymotryptic subfragment 1 (S-1) prepared from rabbit skeletal myosin has lost its ATPase activity upon incubation at 35 degree C for 3 h. The loss in ATPase activity was accompanied by the perturbation of the structure of the 50K domain as indicated by a dramatic increase in the tryptic susceptibility of this domain without any change in the susceptibility of the other domains of S-1. The results indicate that the actin and polyphosphate binding sites of S-1 are distinct and that they are relatively independent of the adenine ring binding site.
ISSN:0006-2960