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Active bound

The activity of Ser/Thr-specific protein kinases is often controlled by autoinhibitory sequences (see 7.1.5). Loss or lack of function of autoregulatory sequences due to an oncogenic mutation can remove Ser/Hir kinase activity bound into mitogenic signaling pathways from normal control and thereby promote tumors. An example is the Raf kinase (see 9.6). Viral v-Raf oncoproteins are characterized by a deletion of the NH2-terminal regulatory sequences. [Pg.434]

Figure 10.17. (a) A typical cyclic GMP standard curve Ca activity bound in the absence of unlabelled cyclic GMP C, = activity bound in the presence of standard or unknown cyclic OMP. standard curve plotting % binding... [Pg.468]

The rate of hydrolysis of esters is dependent upon whether the ester is activated (bound to the metal) or unactivated. For esters that are coordinated to cobalt(III) in a monodentate fashion (Figure 12), the rate of hydrolysis is only accelerated by about 100 times over that of an uncoordinated ester. However, when the ester is coordinated in a bidentate fashion through the amino nitrogen and carbonyl oxygen (Figure 13), the rate of hydrolysis is accelerated by 10 times. " Compared to hydroxide, water does not cause a large increase in the rate of hydrolysis, and it is lO" times slower. ... [Pg.3609]

Endogenous enzymic activity wifi probably not interfere in a solid phase enzyme immunoassay where the activity bound to the solid phase is measured. It is evident that endogenous enzymes can interfere in EMIT-type assays. [Pg.424]

Procedure for Determining Urease Activity Bound to Antibody. It has been shown that the activity of enzymes can simply and readily be determined through the use of potentiometric type electrodes. In previous... [Pg.444]

Noncompetitive ELISA methods are based on sandwich assays, as shown in Figure 6.9. An immobilized primary antibody is present in excess, and quantitatively binds antigen. An enzyme-labeled second antibody is then allowed to react with the bound antigen, forming a sandwich that is detected by measuring enzyme activity bound to the surface of the support. Noncompetitive ELISAs yield calibration curves in which enzyme activity increases with increasing free antigen concentration. [Pg.113]

The SepPak cartridges are preconditioned with 5 mL of ethanol, followed by 5 mL of 0.05M phosphate buffer at pH7.5. An aliquot of the labelled peptide mixed with 10 pL of 50mM DTPA is loaded on the cartridge. The unbound activities °Y, Lu) are eluted with 5 mL of phosphate buffer. The labelled peptide is then eluted with 3 mL of ethanol. The pooled fractions are counted separately, and the radiochemical yield is estimated from the ratio of activity bound to total activity eluted. [Pg.296]

Fig. 8.6. Relationships of the various mathematical models used in immunoassays to the basic general equation as derived by Fernandez et al. (1983). Those used in El A are discussed in detail in Chapter 15. F is the ratio total activity/bound activity, h, and I the concentration of unlabeled and labeled ligand (undiluted), respectively, F the volume of undiluted labeled ligand added to the mixture and Fab the volume of undiluted binder added ab the concentration of binding sites (undiluted) and ab i, the concentration in the incubation mixture. F is the total volume of the incubation mixture. H, the mass of ligand in the incubation mixture. R is the bound/free ratio, h the concentration of unlabeled ligand in the incubation mixture, i the concentration of the standard or unknown, io the concentration of ligand contributed by the label, B bound label and Aobound label at zero standard concentration n is a constant. Fig. 8.6. Relationships of the various mathematical models used in immunoassays to the basic general equation as derived by Fernandez et al. (1983). Those used in El A are discussed in detail in Chapter 15. F is the ratio total activity/bound activity, h, and I the concentration of unlabeled and labeled ligand (undiluted), respectively, F the volume of undiluted labeled ligand added to the mixture and Fab the volume of undiluted binder added ab the concentration of binding sites (undiluted) and ab i, the concentration in the incubation mixture. F is the total volume of the incubation mixture. H, the mass of ligand in the incubation mixture. R is the bound/free ratio, h the concentration of unlabeled ligand in the incubation mixture, i the concentration of the standard or unknown, io the concentration of ligand contributed by the label, B bound label and Aobound label at zero standard concentration n is a constant.
Salts are passively absorbed into wooden objects in seawater, but some ions notably iron(III) are actively bound by cellulose, and high concentrations of iron corrosion products build up in consequence. As the wood becomes anoxic, these salts are converted into sulfides by the activity of SRB. A physical consequence of iron inclusions is that the wood microstructure becomes blocked making the object impermeable to future conservation treatments. Iron sulfide is unstable in the aerobic environment, and its oxidation can destroy the object (Figure 17). [Pg.299]

Activators bound to a distant enhancer can interact with transcription factors bound to a promoter because DNA is flexible and the intervening DNA can form a large loop. [Pg.481]

Ionic strength Protein bound (mg) Activity bound (units) Specific activity (units/ntg)... [Pg.333]


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Activation of cluster-bound carbonyls

Active centre bound

Bound active constraints

Catalytic activity bound enzymes

Cyclic activity, bound lipases

Esters, active polymer-bound

Receptors membrane-bound, activation

Resin-bound catalysts, activity

Surface-bound biocides and activated surfaces

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