Computerized microacidimetric determination of β lactamase Michaelis-Menten constants
نویسندگان
چکیده
منابع مشابه
Single-molecule Michaelis-Menten equations.
This paper summarizes our present theoretical understanding of single-molecule kinetics associated with the Michaelis-Menten mechanism of enzymatic reactions. Single-molecule enzymatic turnover experiments typically measure the probability density f(t) of the stochastic waiting time t for individual turnovers. While f(t) can be reconciled with ensemble kinetics, it contains more information tha...
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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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Phospholipid nanogels enhance the stability and performance of the exoglycosidase enzyme neuraminidase and are used to create a fixed zone of enzyme within a capillary. With nanogels, there is no need to covalently immobilize the enzyme, as it is physically constrained. This enables rapid quantification of Michaelis-Menten constants (KM) for different substrates and ultimately provides a means ...
متن کاملA Comparison of Estimates of Michaelis-menten Kinetic Constants from Various Linear Transformations.
The parameters which characterize this equation, and which must ordinarily be estimated from the observed data, are ‘v,,,, the maximum initial velocity which is theoretically attained when the enzyme has been “saturated” by an infinite concentration of substrate, and K,, the Michaelis constant which is numerically equal to the concentration of substrate for half-maximal initial velocity. Since ...
متن کاملA Comparison of Estimates of Michaelis-Menten Kinetic Constants from Various Linear Transformations
The parameters which characterize this equation, and which must ordinarily be estimated from the observed data, are ‘v,,,, the maximum initial velocity which is theoretically attained when the enzyme has been “saturated” by an infinite concentration of substrate, and K,, the Michaelis constant which is numerically equal to the concentration of substrate for half-maximal initial velocity. Since ...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1973
ISSN: 0014-5793
DOI: 10.1016/0014-5793(73)80154-1