NDLI: Myosin-paramyosin cofilaments: enzymatic interactions with F-actin.

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Myosin-paramyosin cofilaments: enzymatic interactions with F-actin.

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Myosin-paramyosin cofilaments: enzymatic interactions with F-actin.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Aronow, B. J. Epstein, H. F. Harris, H. E.
Abstract	The interaction between paramyosin and myosin has been studied by enzymological methods. Clam adductor paramyosin inhibits the actin-activated, Mg2+-requiring ATPase of both clam adductor and rabbit skeletal muscle myosins. Myosin and paramyosin must be rapidly coprecipitated for this inhibition. Incubation with F-actin in the absence of ATP does not alter this effect. This inhibition follows a hyperbolic function with respect to paramyosin concentration. Slow precipitation by dialysis of myosin and paramyosin together leads to copolymers with actin-activated ATPase equivalent to that of slowly formed myosin filaments. Both kinds of slowly formed filaments have enzymatic properties distinct from those of the rapidly precipitated proteins. Paramyosin is competitive with F-actin for their effects upon myosin. The apparent affinity of myosin for F-actin is markedly reduced by association with paramyosin, but the extrapolated maximal velocity of actomyosin is unaffected. The specificity of this inhibition is strongly suggested by marked quantitative differences between native and cleaved paramyosins. No inhibition of intrinsic myosin ATPase by paramyosin is seen. These studies suggest that at least two types of condition-dependent association between myosin and paramyosin are possible. One class of interactions is associated with enzymic inhibition in rapidly coprecipitated filaments, whereas slowly formed cofilaments exhibit catalytic activity similar to that of identically treat-d myosin and have a characteristic 14.5 nm axial repeat.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	9
Volume Number	73
Language	English
Publisher	National Academy of Sciences
Publisher Date	1976-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Actins Metabolism Adenosine Triphosphatases Myosins Antagonists & Inhibitors Animals Binding, Competitive Bivalvia Chemical Precipitation Kinetics Molecular Weight Myosin Subfragments Protein Binding Rabbits Structure-Activity Relationship Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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