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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 via 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 means of Bacterial pollution (J. Moss and M. Vaughan).

Kinetics of Substrate response in the course of Irreversible amendment of Enzyme job (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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Extra resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 61

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3, consisting again of negative values for AH;, and AC;l but having in this case a positive AGY. It is clear that, not only does the model have the capability of producing the range of phenomena we have seen experimentally, but that the production of such phenomena is an intrinsic and necessary consequence of its nature. In order to examine the ability of the model to answer the questions we have posed, we find it useful to have a more quantitative description of the various kinds of behavior it can generate and of the numerical limits to such phenomena.

2. This arrangement permits us to compare the results of constant temperature binding studies (such as those shown in Fig. 4) with those predicted by the model in a convenient manner. The two heavy solid lines crossing the curves in Fig. 9 indicate the changes in A H " between the enzyme forms for ternary complex formation at 15 and 25°C. While Fig. 9 necessarily 26 HARVEY F. FISHER portrays only a single example of the general model proposed here, and is based on a somewhat arbitrary choice of To parameters, it can nevertheless serve as a basis for exploring the range of phenomena that can be produced by the model and set some limits to the scope of the theory.

39. Grisolia, S . , Biochem. Biophys. Acta, 81,61 (1964). 40. Theorell, H. , Arch. Biochem. , 143, 354 (1971). 41. , J . Phys. , 88, 1257 (1984). 42. , J. Am. Chem. , 49, 28 (1927). 43. Randall, M. , J . Phys. , 45, 959 (1941). 44. , Ann. Rev. Biophys. , 3, 35 (1974). 45. Sturtevant. M.. Prof. Narl. Acad. Sci. USA, 74, 2236 (1977). 46. , Biochemistry, 22, 3384 (1983). 47. , J . Biol. , 256,6381 (1981). 48. , Physiol. , 65, 467 (1985). 49. Kodarna, T. , J . Biol. , 251,7499 (1976). 50. W. , Biochemistry, 20, 2004 (1981).

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