## Abstract The metal ion requirement of myosinβADP binding was investigated by use of Mn^2+^. Mn^2+^ binds to two sets of noninteracting sites on myosin which are characterized by affinity constants of 10^6^ and 10^3^, M^β1^ at 0.016 M KCl concentration. The maximum number of sites is 2 for the hi
On the enthalpy of binding of ADP to heavy meromyosin
β Scribed by Goodno, Charles C. ;Swenson, Charles A.
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1975
- Tongue
- English
- Weight
- 349 KB
- Volume
- 3
- Category
- Article
- ISSN
- 0091-7419
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β¦ Synopsis
Abstract
The binding of ADP to heavy meromyosin has been studied by microcalorimetry. Minute amounts of myokinase interfere with binding measurements, but by selection of appropriate conditions, we can estimate that the value of the apparent ΞH~binding~ lies between β1.0 and β3.0 kcal per mole of ADP bound (0.3 M KCl, 2 mM MgCl~2~, 20 mM Tris, pH 8.00, 20Β°C). Values of ΞH~binding~ reported to date are an order of magnitude larger, and we suggest that these values are artifactual results due to myokinase contamination.
π SIMILAR VOLUMES
## Abstract Heavy meromyosin binding to Fβactin saturated with tropomyosin is studied theoretically. The problem is formulated as a special case of __n__βmer adsorption to a oneβdimensional Ising lattice which is divided into __m__βsiteβlong blocks.
Using a previously described relativistic quantum theory for two particles we calculate the spectrum of bound states of an electron in Coulomb interaction with a heavy ion of charge 2. A spontaneous breakdown of the vacuum does not occur. We do find, however, a critical value of 2 beyond which elect