These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
2. The relationship between steady-state kinetic parameters and equilibrium parameters for one substrate-one product enzymic reactions. Darvey IG J Theor Biol; 1973 Oct; 41(3):441-50. PubMed ID: 4758113 [No Abstract] [Full Text] [Related]
3. The steady-state kinetics of isotope exchange for one substrate-one product enzymic reactions. Darvey IG Biochem J; 1973 Dec; 135(4):861-6. PubMed ID: 4778281 [TBL] [Abstract][Full Text] [Related]
4. The steady-state kinetics of isotope exchange at equilibrium: one substrate-one product enzymic mechanisms where two molecules of substrate or product are bound to an enzyme molecule. Darvey IG Biochem J; 1974 Dec; 143(3):783-4. PubMed ID: 4462758 [TBL] [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 [TBL] [Abstract][Full Text] [Related]
6. A probabilistic approach to compact steady-state kinetic equations for enzymic reactions. Malygin EG; Hattman S J Theor Biol; 2006 Oct; 242(3):627-33. PubMed ID: 16697416 [TBL] [Abstract][Full Text] [Related]
7. Steady-state analysis of kinetic isotope effects in enzymic reactions. Northrop DB Biochemistry; 1975 Jun; 14(12):2644-51. PubMed ID: 1148173 [No Abstract] [Full Text] [Related]
8. One substrate-one product enzymic reactions: the determination of the velocity constants for an enzyme mechanism involving two conformational forms of enzyme and one enzyme intermediate. Darvey IG J Theor Biol; 1977 Jun; 66(4):653-63. PubMed ID: 881850 [No Abstract] [Full Text] [Related]
9. Steady-state parameters of an enzyme from n.m.r. spin transfer with thermal variation. Kuchel PW Biochem J; 1987 May; 244(1):247-8. PubMed ID: 3663116 [TBL] [Abstract][Full Text] [Related]
10. Two rules of enzyme kinetics for reversible Michaelis-Menten mechanisms. Keleti T FEBS Lett; 1986 Nov; 208(1):109-12. PubMed ID: 3770204 [TBL] [Abstract][Full Text] [Related]
11. [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; 14(6):1396-405. PubMed ID: 7442676 [TBL] [Abstract][Full Text] [Related]
13. A generalized theoretical treatment of the transient-state kinetics of enzymic reaction systems far from equilibrium. Pettersson G Acta Chem Scand B; 1978; 32(6):437-46. PubMed ID: 706950 [TBL] [Abstract][Full Text] [Related]
14. Kinetic analysis of chemical or enzymic reactions: an algorithm for the determination of the initial velocity of product formation by the use of a taylor series in reaction time. Rakitzis ET J Theor Biol; 1997 Oct; 188(3):387-9. PubMed ID: 9344744 [No Abstract] [Full Text] [Related]
15. Equations for progress curves of some kinetic models of enzyme-single substrate-single slow binding modifier system. Stojan J J Enzyme Inhib; 1998 Jun; 13(3):161-76. PubMed ID: 9629535 [TBL] [Abstract][Full Text] [Related]
16. [Evaluation of kinetic parameters of unpurified enzymic systems, method for measuring the concentration of endogenous substrate]. Potapov AP Biofizika; 1981; 26(3):434-6. PubMed ID: 7260154 [TBL] [Abstract][Full Text] [Related]
17. Determination of kinetic parameters of enzyme-catalyzed reactions with a minimum number of velocity measurements. Alberty RA J Theor Biol; 2008 Sep; 254(1):156-63. PubMed ID: 18582902 [TBL] [Abstract][Full Text] [Related]
18. Chemical mechanism of a cysteine protease, cathepsin C, as revealed by integration of both steady-state and pre-steady-state solvent kinetic isotope effects. Schneck JL; Villa JP; McDevitt P; McQueney MS; Thrall SH; Meek TD Biochemistry; 2008 Aug; 47(33):8697-710. PubMed ID: 18656960 [TBL] [Abstract][Full Text] [Related]