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2. [Kinetic manifestations of slow isomerization of allosteric enzyme for the model of Monod, Wyman and Changeux]. Kurganov BI; Dorozhko AI; Kagan ZS; Yakovlev VA Biokhimiia; 1975; 40(3):611-21. PubMed ID: 1203376 [TBL] [Abstract][Full Text] [Related]
3. [Deviations from hyperbolic kinetics in slowly dissociating allosteric enzyme systems]. Kuranov BI; Dorozhko AI; Kagan ZS; Iakovlev VA Biokhimiia; 1975; 40(4):793-801. PubMed ID: 1203389 [TBL] [Abstract][Full Text] [Related]
4. Kinetic behavior of associating enzyme systems ofthe type M in equilibrium M2 in equilibrium M3 in equilibrium ... and of the type 2M in equilibrium D in equilibrium D2 in equilibrium D3 in equilibrium .. Kurganov BI Mol Biol; 1975 Jan; 8(4):419-26. PubMed ID: 124013 [TBL] [Abstract][Full Text] [Related]
5. [Theoretical analysis of action of substrate analogs in dissociating enzyme systems]. Kurganov BI Mol Biol (Mosk); 1979; 13(3):649-55. PubMed ID: 460211 [TBL] [Abstract][Full Text] [Related]
7. 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 [TBL] [Abstract][Full Text] [Related]
8. Comparative kinetics of cofactor association and dissociation for the human and trypanosomal S-adenosylhomocysteine hydrolases. 1. Basic features of the association and dissociation processes. Li QS; Cai S; Borchardt RT; Fang J; Kuczera K; Middaugh CR; Schowen RL Biochemistry; 2007 May; 46(19):5798-809. PubMed ID: 17447732 [TBL] [Abstract][Full Text] [Related]
9. [Kinetic properties of sorbitol dehydrogenase from calf liver cell cytoplasm]. Sudovtsov VE; Zharmukhamedova TIu Biokhimiia; 1990 Apr; 55(4):680-6. PubMed ID: 2378913 [TBL] [Abstract][Full Text] [Related]
10. Dissociation of enzyme oligomers: a mechanism for allosteric regulation. Traut TW Crit Rev Biochem Mol Biol; 1994; 29(2):125-63. PubMed ID: 8026214 [TBL] [Abstract][Full Text] [Related]
12. [Comparative theoretic analysis of an open reaction S1 goes to and comes from S2 E(R,T) in which the oligomeric enzyme E(R,T) is isosterically or allosterically activated by the product S2]. Sel'kov EE; Dynnik SN Mol Biol (Mosk); 1978; 12(5):1122-38. PubMed ID: 739997 [TBL] [Abstract][Full Text] [Related]
15. [Generalization of the Monod-Wyman-Changeux model for the case of multisubstrate reactions]. Popova SV; Sel'kov EE Mol Biol (Mosk); 1976; 10(5):1116-26. PubMed ID: 1053074 [TBL] [Abstract][Full Text] [Related]
16. Kinetic analyses of dissociating enzyme systems of the monomer equals dimer equals tetramer and monomer equals tetramer types. Kurganov BI; Yakovlev VA Mol Biol; 1973; 7(3):347-61. PubMed ID: 4797884 [No Abstract] [Full Text] [Related]
17. Pseudocooperative effects in reactivation of membrane-bound enzymes with phospholipids. Cortese JD; Vidal JC Acta Physiol Pharmacol Latinoam; 1984; 34(2):131-42. PubMed ID: 6240912 [TBL] [Abstract][Full Text] [Related]
18. [Substrate inhibition as a cause of oscillations in an open irreversible enzymic reaction S1 + S2 in the presence of E(R,T) leads to S1' + S2'. A mathematical model]. Kaimachnikov NP; Sel'kov EE Biokhimiia; 1977 Apr; 42(4):639-46. PubMed ID: 870087 [TBL] [Abstract][Full Text] [Related]
19. Effects of pH in rapid-equilibrium enzyme kinetics. Alberty RA J Phys Chem B; 2007 Dec; 111(50):14064-8. PubMed ID: 18027926 [TBL] [Abstract][Full Text] [Related]
20. Kinetic analysis of enzyme inhibition by substrate depletion. Cortese JD; Vidal JC Acta Physiol Lat Am; 1981; 31(3):161-71. PubMed ID: 7187587 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]