Michaelis-Menten kinetic analysis ofEscherichia coliSS142 adhesion to intestine 407 monolayers
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چکیده
منابع مشابه
Kinetic analysis of multisite phosphorylation using analytic solutions to Michaelis-Menten equations.
Phosphorylation-induced expression or modulation of a functional protein is a common signal in living cells. Many functional proteins are phosphorylated at multiple sites and it is frequently observed that phosphorylation at one site enhances or suppresses phosphorylation at another site. Therefore, characterizing such cooperative phosphorylation is important. In this study, we determine a temp...
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The summation of the effects of two or more reversible inhibitors of various types on the initial velocity of enzyme systems obeying Michaelis-Menten kinetics is described by the the general relation: (formula: see text) wherein v1,2,3...n is the velocity of reaction in the simultaneous presence of n inhibitors, vi is the velocity observed in the presence of each individual inhibitor, and v0 is...
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We study chemical reactions with complex mechanisms under two assumptions: (i) intermediates are present in small amounts (this is the quasi-steady-state hypothesis or QSS) and (ii) they are in equilibrium relations with substrates (this is the quasiequilibrium hypothesis or QE). Under these assumptions, we prove the generalized mass action law together with the basic relations between kinetic ...
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Most biological processes are controlled by complex systems of enzymatic chemical reactions. Although the majority of enzymatic networks have very elaborate structures, there are many experimental observations indicating that some turnover rates still follow a simple Michaelis-Menten relation with a hyperbolic dependence on a substrate concentration. The original Michaelis-Menten mechanism has ...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1981
ISSN: 0378-1097,1574-6968
DOI: 10.1111/j.1574-6968.1981.tb07620.x