Some properties of cross-linked polymers of glutamic dehydrogenase.
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Animals↗
Biomedical subjects
E Reisler
Publications and source records attributed to E Reisler.
Myosin ATP hydrolysis: a mechanism involving a magnesium chelate complex.
It is suggested that under physiological conditions (> 1 mM Mg(2+)) MgATP binds to myosin to form a chelate involving the two reactive sulfhydryl sites (SH(1) and SH(2)). The stability of the chelate structure results in marked inhibition of the myosin ATPase in the presence of millimolar magnesium ion. The inhibitory effect of magnesium ion can be eliminated chemically by blocking either the SH(1) or SH(2) site since this precludes formation of the chelate. In muscle, actin apparently behaves in a similar fashion in that its interaction with myosin causes a disruption of the chelate structure.
Adenosine Triphosphatases↗
Crosslinking of myosin and myosin filaments.
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Actins↗
Solubility of toluene in bovine liver glutamate dehydrogenase solutions and enhancement of enzyme association.
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Animals↗
Bovine liver glutamate dehydrogenase association and dependence of association on temperature.
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Animals↗
Angular dependence of scattered light, rotary frictional coefficients, and distribution of sizes of associated oligomers in solutions of bovine liver glutamate dehydrogenase.
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Animals↗
Molecular weights, association, and frictional resistance of bovine liver glutamate dehydrogenase at low concentrations. Equilibrium and velocity sedimentation, light-scattering studies, and settling experiments with macroscopic models of the enzyme oligomer.
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Animals↗
Studies on the viscosity of solutions of bovine liver glutamate dehydrogenase and on related hydrodynamic models; effect of toluene on enzyme association.
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Animals↗
Interpretation of equilibrium sedimentation measurements of proteins in guanidine hydrochloride solutions. Partial volumes, density increments, and the molecular weight of the subunits of rabbit muscle aldolase.
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Animals↗