Polyphasic Character of ATP Hydrolysis in Actomyosin System
نویسندگان
چکیده
منابع مشابه
Thermodynamic aspects of ATP hydrolysis of actomyosin complex
Directional movement of cellular components is essential to all eukaryotic cells, and is driven by a mechanoenzymatic system consisting largely of the actin– myosin cytoskeletal protein complex. Structural and functional analysis of this complex has provided critical insights into the mechanisms that enforce and regulate the movement of intracellular components such as muscle fibers, vesicles, ...
متن کاملMechanism of adenosine triphosphate hydrolysis by actomyosin.
The hydrolysis of ATP by acto-HMM has been studied during the transient state using a rapid-mixing apparatus. The rate of substrate binding was slightly slower and the rate of hydrolysis of the first molecule of ATP was essentially the same as for heavy meromyosin (HMM) alone. The rate of acto-HMM dissociation after binding substrate was too fast to measure in a stopped-flow apparatus, conseque...
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چکیده پلاتین، فلزی نجیب، پایدار و گران قیمت با خاصیت کاتالیزوری زیاد است که کاربرد های صنعتی فراوانی دارد. کمپلکس های پلاتین(ii) به عنوان دارو های ضد سرطان شناخته شدند و در شیمی درمانی بیماران سرطانی کاربرد دارند. خاصیت کاتالیزوری و عملکرد گزینشی پلاتین مستقیماً به اندازه و- شکل ماده ی پلاتینی بستگی دارد. بعضی از نانو ذرات فلزی در سطح مشترک مایع- مایع سنتز شده اند، اما نانو ساختار های پلاتین ب...
Tropomyosin-troponin-induced changes in the partitioning of free energy release of actomyosin-catalyzed ATP hydrolysis as measured by ATP-phosphate exchange.
ATPase activity and ATP-Pi exchange of unregulated (without tropomyosin-troponin) and regulated (with tropomyosin-troponin) acto-HMM were measured in media containing 0.2 mg/ml actin, HMM, and (when present) tropomyosin-troponin, 2 mM MgCl2, 10 mM KCl, 2 mM NaN3, 10 mM Pi (pH 7.0), 3 MM ATP. The following mean values for ATPase activity and for the rate of incorporation of Pi into ATP (each per...
متن کاملZooming in on ATP hydrolysis in F1.
We summarize our current view of the reaction mechanism in F(1)-ATPase as it has emerged from experiment, theory, and computational studies over the last several years. ATP catalysis in the catalytic binding pockets of F(1) takes place without the release of any significant free energy and is efficiently driven by the combined action of two water molecules utilizing a so-called protein-relay me...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1979
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1979.tb19747.x