175 related articles for article (PubMed ID: 3190712)
1. Rigorous determination of the Hill coefficient of non-Michaelian substrate-inhibited enzymes.
Bounias M
Biochem Int; 1988 Jul; 17(1):147-54. PubMed ID: 3190712
[TBL] [Abstract][Full Text] [Related]
2. [Determination of kinetic constants in the general case of cooperative type or Michaelis enzymes inhibited by their substrate: theoretic analysis].
Bounias M
C R Acad Sci III; 1986; 303(12):495-500. PubMed ID: 3098357
[TBL] [Abstract][Full Text] [Related]
3. A graphical method for determining inhibition constants.
Yoshino M; Murakami K
J Enzyme Inhib Med Chem; 2009 Dec; 24(6):1288-90. PubMed ID: 19912063
[TBL] [Abstract][Full Text] [Related]
4. [Specific ligand induced dimerization of allosteric enzymes].
Kurganov BI
Mol Biol (Mosk); 1982; 16(2):424-33. PubMed ID: 7073865
[TBL] [Abstract][Full Text] [Related]
5. Inhibition and activation of enzymes. The effect of a modifier on the reaction rate and on kinetic parameters.
Fontes R; Ribeiro JM; Sillero A
Acta Biochim Pol; 2000; 47(1):233-57. PubMed ID: 10961698
[TBL] [Abstract][Full Text] [Related]
6. [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]
7. 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]
8. Advantages of continuous over batch reactors for the kinetic analysis of enzymes inhibited by an unknown substrate impurity.
Gallifuoco A; Alfani F; Cantarella M
Biotechnol Bioeng; 2002 Sep; 79(6):641-6. PubMed ID: 12209811
[TBL] [Abstract][Full Text] [Related]
9. [Description of the ratios between metabolite concentrations in a polyenzyme system].
Stefanov VE; Magarshak IuB
Biofizika; 1979; 24(6):999-1002. PubMed ID: 508840
[TBL] [Abstract][Full Text] [Related]
10. [Enzyme inactivation in the reaction process. Regulatory role].
Varfolomeev SD
Biokhimiia; 1984 May; 49(5):723-35. PubMed ID: 6743701
[TBL] [Abstract][Full Text] [Related]
11. [Self-oscillations in an open biochemical substrate-inhibited reaction interacting with the enzyme-producing system].
Nazarenko VG; Sel'kov EE
Biofizika; 1981; 26(3):428-33. PubMed ID: 7260153
[TBL] [Abstract][Full Text] [Related]
12. Experimental evidence for allosteric modifier saturation as predicted by the bi-substrate Hill equation.
Hanekom AJ; Hofmeyr JH; Snoep JL; Rohwer JM
Syst Biol (Stevenage); 2006 Sep; 153(5):342-5. PubMed ID: 16986313
[TBL] [Abstract][Full Text] [Related]
13. The use of isotope effects to determine enzyme mechanisms.
Cleland WW
Arch Biochem Biophys; 2005 Jan; 433(1):2-12. PubMed ID: 15581561
[TBL] [Abstract][Full Text] [Related]
14. [The influence of data errors on numerical estimation of kinetic constants in allosteric models].
Geier T; Reich JG
Acta Biol Med Ger; 1972; 29(6):793-804. PubMed ID: 4633697
[No Abstract] [Full Text] [Related]
15. [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]
16. Kinetic analysis of modification reactions at comparable enzyme and modifier concentrations.
Zhao KY; Wang ZX
J Theor Biol; 1996 Aug; 181(4):319-27. PubMed ID: 8949580
[TBL] [Abstract][Full Text] [Related]
17. Intermolecular ligand substitution reactions.
Jenkins WT
Prog Clin Biol Res; 1984; 144B():89-96. PubMed ID: 6718418
[TBL] [Abstract][Full Text] [Related]
18. A graphical method for determining inhibition parameters for partial and complete inhibitors.
Yoshino M
Biochem J; 1987 Dec; 248(3):815-20. PubMed ID: 3435487
[TBL] [Abstract][Full Text] [Related]
19. Apparent co-operativity for highly concentrated Michaelian and allosteric enzymes.
Laurent M; Kellershohn N
J Mol Biol; 1984 Apr; 174(3):543-55. PubMed ID: 6716486
[TBL] [Abstract][Full Text] [Related]
20. A simple method for calculating Km and V from a single enzyme reaction progress curve.
Yun SL; Suelter CH
Biochim Biophys Acta; 1977 Jan; 480(1):1-13. PubMed ID: 831830
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
