By Alton Meister

A Unifying version of the Thermodynamics of Formation of Dehydrogenase-Ligand Complexes (H. Fisher).

Sorbitol Dehydrogenase (J. Jeffery and H. Jornvall).

Molecular measurement choice of Enzymes through Radiation Inactivation (E. Kempner).

Calcineurin (C. Klee, et al).

The habit and importance of Slow-Binding Enzyme Inhibitors (J. Morrison and C. Walsh).

ADP-Ribosylation of Guanyl Nucleotide-Binding Regulatory Proteins by way of Bacterial pollutants (J. Moss and M. Vaughan).

Kinetics of Substrate response in the course of Irreversible amendment of Enzyme task (C. Tsou).

The Dynamics of DNA Polymerase-Catalyzed Reactions (V. Mizrahi and S. Benkovic).

writer Index.

topic Index.

Cummulative Indexes, Vols 1-61.Content:

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18). 39 40 HARVEY F. FISHER denaturation experiments provide the strongest direct evidence that the existence of a duality of enzyme forms and that the genera1 relationships between those forms proposed here do indeed correspond (at least in a qualitative manner) to the physical reality in the glutamate dehydrogenase system. D. CRYOGENIC OBSERVATIONS Some time ago we reported that under cryogenic conditions (50% methanol, - 42°C) one can observe two different forms of glutamate dehydrogenase and two different forms of each complex occurring on the reaction pathway.

MACROSTATE-SHIFT MODELS FOR THE MUSCLE ATPase SYSTEM Kodama has proposed a mechanism for the muscle myosidactin ATPase system which involves a series of linked two-state interconversions and which thus resembles the general model described here (48). Indeed, Kodama uses the interpretation of AC, effects as proposed by Eftink and Biltonen (46) and Fisher et al. (13) to formulate his hypothesis. In addition to the calorimetrically determined temperature-dependent A Cp’s he has observed (49) Kodama also cites the insightful paper of Shriver and Sykes (50), whose NMR studies led them to propose a model for myosin ATPase in which a step involving the interconversion of two macrostates actually provides the “power stroke” which drives the catalytic reaction.

Thus, it appears that while both AC,,,’s and AGP’s vary from positive to negative values and while the To’s of the binary complexes can have almost any value, yet the ternary complexes are all almost energetically identical-the mere formation of the ternary complex itself drives the enzyme to a single form with properties quite unlike that of any binary complex. The ability of the model to predict a bounded region that encompasses all of the experimental points is a necessary, but hardly a very demanding test.

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