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162 related items for PubMed ID: 7695087
1. Kinlsq: a program for fitting kinetics data with numerically integrated rate equations and its application to the analysis of slow, tight-binding inhibition data. Gutheil WG, Kettner CA, Bachovchin WW. Anal Biochem; 1994 Nov 15; 223(1):13-20. PubMed ID: 7695087 [Abstract] [Full Text] [Related]
2. The comparison of the estimation of enzyme kinetic parameters by fitting reaction curve to the integrated Michaelis-Menten rate equations of different predictor variables. Liao F, Zhu XY, Wang YM, Zuo YP. J Biochem Biophys Methods; 2005 Jan 31; 62(1):13-24. PubMed ID: 15656940 [Abstract] [Full Text] [Related]
3. Exact and approximate solutions for the decades-old Michaelis-Menten equation: Progress-curve analysis through integrated rate equations. Goličnik M. Biochem Mol Biol Educ; 2011 Jan 31; 39(2):117-25. PubMed ID: 21445903 [Abstract] [Full Text] [Related]
4. Application of the Van Slyke-Cullen irreversible mechanism in the analysis of enzymatic progress curves. Kuzmic P. Anal Biochem; 2009 Nov 15; 394(2):287-9. PubMed ID: 19627979 [Abstract] [Full Text] [Related]
5. Interpreting complex binding kinetics from optical biosensors: a comparison of analysis by linearization, the integrated rate equation, and numerical integration. Morton TA, Myszka DG, Chaiken IM. Anal Biochem; 1995 May 01; 227(1):176-85. PubMed ID: 7668379 [Abstract] [Full Text] [Related]
6. Explicit analytic approximations for time-dependent solutions of the generalized integrated Michaelis-Menten equation. Goličnik M. Anal Biochem; 2011 Apr 15; 411(2):303-5. PubMed ID: 21241654 [Abstract] [Full Text] [Related]
7. A simple computer program with statistical tests for the analysis of enzyme kinetics. Brooks SP. Biotechniques; 1992 Dec 15; 13(6):906-11. PubMed ID: 1476744 [Abstract] [Full Text] [Related]
8. Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase. Kuzmic P. Anal Biochem; 1996 Jun 01; 237(2):260-73. PubMed ID: 8660575 [Abstract] [Full Text] [Related]
9. Estimation of kinetic parameters for enzyme-inhibition reaction models using direct time-dependent equations for reactant concentrations. Goličnik M. Acta Chim Slov; 2012 Mar 01; 59(1):207-11. PubMed ID: 24061194 [Abstract] [Full Text] [Related]
10. Sigmoidal substrate saturation curves in Michaelis-Menten mechanism as an artefact. Fischer E, Keleti T. Acta Biochim Biophys Acad Sci Hung; 1975 Mar 01; 10(3):221-7. PubMed ID: 1211106 [Abstract] [Full Text] [Related]
11. The integrated Michaelis-Menten rate equation: déjà vu or vu jàdé? Goličnik M. J Enzyme Inhib Med Chem; 2013 Aug 01; 28(4):879-93. PubMed ID: 22630075 [Abstract] [Full Text] [Related]
12. Explicit reformulations of time-dependent solution for a Michaelis-Menten enzyme reaction model. Golicnik M. Anal Biochem; 2010 Nov 01; 406(1):94-6. PubMed ID: 20599638 [Abstract] [Full Text] [Related]
13. A simple method for determining kinetic constants of slow, tight-binding inhibition. Wang ZX. Anal Biochem; 1993 Sep 01; 213(2):370-7. PubMed ID: 8238913 [Abstract] [Full Text] [Related]
14. Analysis of binding of monoclonal antibody to a malarial peptide by surface plasmon resonance biosensor and integrated rate equations. Wohlhueter RM, Parekh K, Udhayakumar V, Fang S, Lal AA. J Immunol; 1994 Jul 01; 153(1):181-9. PubMed ID: 8207235 [Abstract] [Full Text] [Related]
15. Enzyme kinetics at high enzyme concentration. Schnell S, Maini PK. Bull Math Biol; 2000 May 01; 62(3):483-99. PubMed ID: 10812718 [Abstract] [Full Text] [Related]
16. Enzymatic reaction of silent substrates: kinetic theory and application to the serine protease chymotrypsin. Case A, Huskey WP, Stein RL. Biochemistry; 2003 Apr 29; 42(16):4727-32. PubMed ID: 12705836 [Abstract] [Full Text] [Related]
17. Slow-binding inhibition of gamma-aminobutyric acid aminotransferase by hydrazine analogues. Lightcap ES, Silverman RB. J Med Chem; 1996 Feb 02; 39(3):686-94. PubMed ID: 8576911 [Abstract] [Full Text] [Related]
18. A two-step computer-assisted method for deriving steady-state rate equations. Fromm SJ, Fromm HJ. Biochem Biophys Res Commun; 1999 Nov 19; 265(2):448-52. PubMed ID: 10558887 [Abstract] [Full Text] [Related]
19. Surface enzyme kinetics for biopolymer microarrays: a combination of Langmuir and Michaelis-Menten concepts. Lee HJ, Wark AW, Goodrich TT, Fang S, Corn RM. Langmuir; 2005 Apr 26; 21(9):4050-7. PubMed ID: 15835973 [Abstract] [Full Text] [Related]
20. A new graphical method for determining parameters in Michaelis-Menten-type kinetics for enzymatic lactose hydrolysis. Yang ST, Okos MR. Biotechnol Bioeng; 1989 Sep 26; 34(6):763-73. PubMed ID: 18588163 [Abstract] [Full Text] [Related] Page: [Next] [New Search]