1983
DOI: 10.1111/j.1432-1033.1983.tb07551.x
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The Role of Magnesium in Binding of the Nucleotide Polyphosphate Chain to the Active Site of Myosin Subfragment‐1

Abstract: The binding of adenosine 5'-[P,y-imidoltriphosphate, pyrophosphate and triphosphate to the active site of myosin subfragment-I was assessed in the presence and absence of Mg2+ by direct and indirect methods. In addition, the affinity and stoichiometry of Mg2+ in the ternary complexes formed by protein, Mg2+ and each of these phosphate compounds have been determined. As direct methods, equilibrium dialysis, sedimentation and quantitative affinity chromatography were used in conjunction with the indirect method … Show more

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Cited by 7 publications
(2 citation statements)
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“…Just as Perry & Grey (1956) theorized about PPi inhibition of ATPase, PPi inhibition of TPPase activity could be due to the increased amount of PPi inhibiting the hydrolysis of TPP through product inhibition. Schaub et al (1983) reported that the binding constant (K d ) for Mg-PPi is 0.37 μM, which shows that PPi binds tightly to the enzyme. This high affinity binding constant and the measured K i values strongly suggest that PPi is a strong competitive inhibitor of TPPase activity.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…Just as Perry & Grey (1956) theorized about PPi inhibition of ATPase, PPi inhibition of TPPase activity could be due to the increased amount of PPi inhibiting the hydrolysis of TPP through product inhibition. Schaub et al (1983) reported that the binding constant (K d ) for Mg-PPi is 0.37 μM, which shows that PPi binds tightly to the enzyme. This high affinity binding constant and the measured K i values strongly suggest that PPi is a strong competitive inhibitor of TPPase activity.…”
Section: Discussionmentioning
confidence: 99%
“…Pi is released first, then PPi dissociates. Relative to TPP, the binding constant of PPi is higher (Schaub, Watterson, Loth, & Foletta, 1983). Considering this fact, PPi is likely a competitive inhibitor for the myosin TPPase and PPi has been shown to inhibit TPP hydrolysis in meat homogenates (Neraal & Hamm, 1977a).…”
Section: Introductionmentioning
confidence: 99%