Psychoaktive Pilze - Bestimmungskarten by Jochen Gartz

By Jochen Gartz

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Therefore, the affinity of the chemical reaction may be expressed as A = F A + p -~pc = p i + & - p: - RTln Q. 15) Moreover, the standard free energy difference, AGO, is defined as AGO = p: - ( p i + p:) = -RT In K . 17) and the net reaction rate, or the flow per unit volume, assumes the form v = Jv= k[AI[B]{ 1 - exp(-A/RT)}. 18) This equation shows that there is an exponential relationship between the flow and the force that generates the flow. 19) 18 and eq. 20) The flow-force relationship is thus linear close to thermodynamic equilibrium.

Effect of MgATP, MgADP and glucose-6phosphate on co-operativity of wheat germ hexokinase LI. A - Effect of MgADP. B - Effect of glucose-6-phosphate. C -Effect of MgADP. Adapted from ref. [57]. 50 and MgADP) in a compulsory, or preferred, order pathway, glucose being bound first and glucose-6-phosphatereleased last. The enzyme has only one binding site for glucose. However, under steady state conditions, the enzyme displays negative co-operativityrelative to glucose and no co-operativitywith respect to ATP (Fig.

A structure “complementary” to that of the ligand. In Fig. 4 above, this process is pictured by the conversion of a circle into a square. As the free enzyme occurs in its “circle” and not in its “square” state, one is led to the conclusion that the free energy of this ideal conformational transition, A G c , can only be positive. The second ideal process corresponds to the binding 29 of the ligand to the “complementary”,distorted, active site. Its free energy is AGB and may be positive or negative.

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