Enzymes conservation

Substituting the enzyme conservation Equation A17.1 in the left-hand side of Equation A17.2 yields... 

The equilibrium between the free and bound enzyme is given by the enzyme conservation equation,... 

To determine how the concentrations of the substrate, product, and enzyme-substrate complex are changing with time, we can solve Eqs. (2.14), (2.30), and (2.31) with the enzyme conservation equation Eq. (2.9) by using ACSL. 

Figure 3. Linear representations the Arabidopsis thaliana At) PI4Ks in comparison to human IIs) isoforms. Thus far, only the type III 4/PI4K.S have been shown to be functional enzymes. Conserved domains are indicated and described in the text.

This, the enzyme conservation equation , simply indicates that the total enzyme concentration in all forms, e, remains constant. If we substitute for E from Eqn. la, we obtain... 

If we now want to work out the initial-rate equation for this inhibition scheme, the equation (la or lb) relating [E] to [EA] still stands unaltered, as does Eqn. 3 relating v to [EA], What has to expand, however, is Eqn. 2, the enzyme conservation equation, since we now have a third enzyme species, El, to consider. We thus need an equation relating [Elj to the concentrations of the other enzyme forms. Since the route from E to El is a dead end , we may assume that equilibrium is established between E, I and El. This will be governed by a dissociation constant K-, so that we may write... 

Since protolytic reactions are usually very fast (especially in the presence of buffers, where proton-transfer reactions occur readily), all the protolytic steps can be assumed to be in equilibrium throughout the course of the reaction. The derivation of the rate equation is exactly as before except that the enzyme-conservation equation is given by... 

The total activity of the enzyme does not change during a valid assay, which is also termed the enzyme conservation expression ... 

In France, the research was initiated in the mid-sixties in Rouen. The special technique developed [22, 35, 36, 37] uses the reticulating cross-links, with e.g. glutaralde-hyde, between enzymes and other proteins such as human albumin (for medical uses) or bovin albumin or gelatin or collagen when mechanical properties are of more importance. Analogous methods have been employed by Quiocho and Richards [38] to link enzymes in the solid state for spectroscopic studies. It appears that at least one of the first series of a variety of non-proteolytic enzymes conserving a high fraction... 

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