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4. A theoretical model for calculation of the rate constant of enzyme-substrate complex formation. 3. Effect of intermolecular forces and diffusion motion of the enzyme molecule on the rate constant. Somogyi B. Acta Biochim Biophys Acad Sci Hung; 1974; 9(3):185-96. PubMed ID: 4419764 [No Abstract] [Full Text] [Related]
5. Synergism of substrate binding with enzymes, as observed by equilibrium isotope exchange kinetics: model patterns. Wedler FC. Physiol Chem Phys; 1978; 10(2):97-106. PubMed ID: 724812 [Abstract] [Full Text] [Related]
6. Measurement of dissociation constants of inhibitors binding to Src SH2 domain protein by non-covalent electrospray ionization mass spectrometry. Bligh SW, Haley T, Lowe PN. J Mol Recognit; 2003; 16(3):139-48. PubMed ID: 12833569 [Abstract] [Full Text] [Related]
8. A graphical method for determining the number of essential sites in enzymes with multiple binding sites for a ligand. Wang ZX, Srivastava DK. Anal Biochem; 1994 Jan; 216(1):15-26. PubMed ID: 8135345 [Abstract] [Full Text] [Related]
9. Kinetic analysis of enzyme inhibition by substrate depletion. Cortese JD, Vidal JC. Acta Physiol Lat Am; 1981 Jan; 31(3):161-71. PubMed ID: 7187587 [Abstract] [Full Text] [Related]
11. A theoretical model for calculation of the rate constant of enzyme-substrate complex formation. I. Calculation of rate constant in the case of motionless enzyme molecule without nonspecific intermolecular forces. Somogyi B, Damjanovich S. Acta Biochim Biophys Acad Sci Hung; 1973 Jan; 8(3):153-60. PubMed ID: 4784598 [No Abstract] [Full Text] [Related]
12. A theoretical model for calculation of the rate constant of enzyme-substrate complex formation. II. Effect of intermolecular forces on the parameters describing the translational diffusion motion of a particle. Somogyi B. Acta Biochim Biophys Acad Sci Hung; 1974 Jan; 9(3):175-84. PubMed ID: 4419763 [No Abstract] [Full Text] [Related]
13. Mechanisms of stabilization of the insulin hexamer through allosteric ligand interactions. Rahuel-Clermont S, French CA, Kaarsholm NC, Dunn MF, Chou CI. Biochemistry; 1997 May 13; 36(19):5837-45. PubMed ID: 9153424 [Abstract] [Full Text] [Related]
14. Allosteric regulation of biosynthetic threonine deaminase from Escherichia coli: effects of isoleucine and valine on active-site ligand binding and catalysis. Eisenstein E. Arch Biochem Biophys; 1995 Jan 10; 316(1):311-8. PubMed ID: 7840631 [Abstract] [Full Text] [Related]
17. [Enzyme inactivation in the reaction process. Regulatory role]. Varfolomeev SD. Biokhimiia; 1984 May 10; 49(5):723-35. PubMed ID: 6743701 [Abstract] [Full Text] [Related]
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19. [Relationship between the apparent order of substrate binding to an enzyme and the nature of the reaction between their active centers]. Iashina LN, Malygin EG, Zinov'ev VV. Mol Biol (Mosk); 1980 Feb 10; 14(6):1396-405. PubMed ID: 7442676 [Abstract] [Full Text] [Related]
20. Ligand dissociation constants from competition binding assays: errors associated with ligand depletion. Goldstein A, Barrett RW. Mol Pharmacol; 1987 Jun 10; 31(6):603-9. PubMed ID: 3600604 [Abstract] [Full Text] [Related] Page: [Next] [New Search]