Literature DB >> 738273

The rate of release of ATP from its complex with myosin.

J W Cardon, P D Boyer.   

Abstract

An approach previously published from this laboratory for measurement of the rate of dissociation of ATP from its complex with myosin has been carefully evaluated. The procedure has been found valid, and the off constant (21 degrees C, 1=0.21 M, pH 7.0) is 1x 10(-4)s(-1). Other data for the rate of ATP binding give a Kd for myosin ATP of 6x10(-11) M. Reasons for the apparent discrepancy between this value and that reported by others have been examined. When various factors are appropriately taken into account, this discrepancy is eliminated.

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Year:  1978        PMID: 738273     DOI: 10.1111/j.1432-1033.1978.tb12765.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  3 in total

1.  The ATPase kinetics of insect fibrillar flight muscle myosin subfragment-1.

Authors:  D C White; R W Zimmerman; D R Trentham
Journal:  J Muscle Res Cell Motil       Date:  1986-04       Impact factor: 2.698

Review 2.  Using optical tweezers to relate the chemical and mechanical cross-bridge cycles.

Authors:  Walter Steffen; John Sleep
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2004-12-29       Impact factor: 6.237

3.  Modification of the interactions of myosin with actin and 5'-adenylyl imidodiphosphate by substitution of ethylene glycol for water.

Authors:  S B Marston; R T Tregear
Journal:  Biochem J       Date:  1984-01-01       Impact factor: 3.857

  3 in total

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