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 dimension selection 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 via Bacterial pollution (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).
Cummulative Indexes, Vols 1-61.Content:
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Additional resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 61
The two heavy lines connecting the individual curves indicate the temperature-dependent AH contribution for the various forms that would be observed in conventional isothermal measurements at 25 and at 15°C. ) Conforming to the assumptions listed previously, the curves are calculated assuming that A H ; is 22 kca! -' in each case, but that each enzyme form (and therefore each curve) has its own unique value of To as indicated above the curve. The set of five curves representing isomerizations of E, EA, EAB, EB, and a repetition of E are arranged in the same order as they occur in the energetic profile in Fig.
This is just the pattern that would be expected for a set of systems each of which involves an E E' equilibrium where only the E' forms denature (under these experimental conditions); where all E' forms denature at the same intrinsic rate; and where the equilibrium constants for the E $ E' reaction differ substantially among themselves. * These two features of the thermal * It should be noted that the To is not the T , (the melting point of denaturation). In general, To appears to lie at least 20" below the T,.
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