Übersetzung für "Enzymkinetik" in Englisch

Enzyme kinetics was more poetic than Bearing's class.

He is known mainly as an early pioneer in enzyme kinetics.

The reaction thereby obeys the known laws of enzyme kinetics.

Thus, Bodenstein contributed to early research in enzyme kinetics.

There are many practical uses of enzyme kinetics.

For this, firstly the optimum restriction incubation duration was determined by recording enzyme kinetics.

The presence of perindopril makes it possible to induce kinase II inhibition in the body of the enzyme in the body.

Cantley obtained his Ph.D. at Cornell University in Ithaca, New York, where he worked with Gordon Hammes on enzyme kinetics, using FRET to study enzyme conformational changes.

Furthermore, said activity measurement can be carried out in a continuous manner, i.e. over a longer period of time, thus allowing to obtain valuable information in relation to enzyme kinetics.

By the end of the 19th century the concept of enzymes was well established, though equations of chemical kinetics would not be applied to enzymatic reactions until the early 20th century.

Another important term in enzyme kinetics is K cat . This is simply a measure of the efficiency of the enzyme, or how much product it can produce in one second.

The wavelength range of 340 to 850 nm makes the MultiskanTM FC suited to applications from enzyme kinetics to Lowry assays.

Enzyme kinetics involves the measurement of the rate at which chemical reactions that are catalyzed by enzymes occur.

The maximum reaction rate of the substrate in the body of the individual is determined via a change of the measured 13 CO 2 content in the air exhaled by the individual using zero-order enzyme kinetics.

The method is characterized by using a measuring device, the maximum reaction rate of the substrate in the body of the individual being determined via a change of the measured 13 CO 2 content in the air exhaled by the individual using zero-order enzyme kinetics.

The designations “KM value” or “Michaelis-Menten constant” relate to a parameter for describing the enzymatic affinity of the units ?M or mM, which are calculated with the help of the linear Hanes plots according to H. Bisswang (2002, Enzyme Kinetics, ISBN 3-527-30343-X, page 19), wherein the function “enzyme kinetics, single substrate” in the SigmaPlot 12.0 program is preferably used for this purpose.

The designations “catalytic constant of the enzyme reaction” or “k cat value” relate to a parameter for describing the conversion rate of a polypeptide and/or enzyme, which is given in s ?1 and is preferably calculated with the help of the “enzyme kinetic, single substrate” function of the SigmaPlot 12.0 program.

The designations “catalytic constant of the enzyme reaction” or “kcat value” relate to a parameter for describing the conversion rate of a polypeptide and/or enzyme, which is given in s?1 and is preferably calculated with the help of the “enzyme kinetic, single substrate” function of the SigmaPlot 12.0 program.

The “maximum enzyme rate” or “vmax value” is given in units of ?M/s or mM/s and is determined with the help of the linear Hanes plot by analogy with the KM value, wherein the function “enzyme kinetic, single substrate” of the SigmaPlot 12.0 program is preferably used for this.

The person skilled in the art knows that the pH value has crucial impact on enzyme kinetics and, thus, on the time flow of enzymatic reactions.

This permits the actual quantitative expressiveness, since zero-order enzyme kinetics are achieved, and only this permits a statement concerning the maximum functional capacity of an enzyme system.

In particular, all matters having to do with the chemical equilibrium of the conversion of isomaltulose to 1,6-GPS require operation with isolated enzymes, since otherwise the stoichiometry, dissociation constants, matters of inhibition or activation of the enzyme, problems of cooperativity, initial rate, conformation, ligands and all other problems of enzyme kinetics and the binding data of interest cannot be analyzed with sufficient precision.

The determination of the enzyme kinetics of the native form of the xylose isomerase resulted in a K m value of 61.85±3.41 mM and for the codon-optimized form a K m value of 66.01±1 mM (FIG.