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Product saturation curve

Parker and Lenhard (1989) and Lenhard and Parker (1988) have developed equations that relate the apparent product thickness measured at a well under equilibrium conditions with the product and water saturations in a vertical column of soils adjacent to the well. By integrating the product saturation curve with respect to elevation, an equivalent depth of LNAPL-saturated pores is obtained. This process has been implemented in a computer program called OILEQUIL. The result is reported as a total oil depth in a vertical profile. The water and oil saturation curves with elevation can also be produced and printed in graphical or tabular form. [Pg.184]

Top typical saturation curve and variation of mean electron energy with applied field. Middle fraction of the electron swarm exceeding the specific energy at each field strength. Calculated assuming constant collision cross-section and Maxwell-Boltzman distribution. Bottom variation of products typical of involvement of ionic precursors (methane) and excited intermediates (ethane) with applied field strength... [Pg.254]

The first product of nitrosyl transfer to nitrite in Eq. (2), E N203, contains N-N bonded N2O3 which is itself a well-known and powerful nitrosyl donor. It is reasonable to suppose therefore that nitrosyl transfer reactions with N- and O-nucleophiles could involve both E NO (or E HONO) and E N205. In addition, the involvement of a second molecule of nitrite for denitrification would require that the substrate saturation curve should be sigmoidal to reflect a term second-order in nitrite concentration. No such effect has been reported to our knowledge. The use of bimolecular substrate kinetics in dilute solutions to generate an intermediate subject to solvolysis seems metabolically unwise hut not impossible. [Pg.296]

The kinetics of the lytic effect displayed by the complexes of immobilized heparin with thrombin and fibrinogen, in distinction from those with plasmin, are described by their saturation curves. The observed slowing down of the dissolution of unstabilized fibrin is probably due to the inhibiton of the lytic activity of the complexes by the soluble products of the reaction. In fact, as it was shown in Ref. 106, further addition of immobilized heparin-protein complex to partially hydrolyzed fibrin results in a complete recovery of the dissolution rate. [Pg.126]

In this equation, a hyperbolic saturation curve is described by two constants, Vm and Km. In the simple example in Figure IB, v is velocity, Vm is simply [EJ and Km is (k2 + 23) 12- Umax (or Vm) is the reaction velocity at saturating concentrations of substrate, and Km is the concentration of the substrate that achieves half the maximum velocity. Although the constant Km is the most useful descriptor of the affinity of the substrate for the enzyme, it is important to note the difference between Km and Kh. Even for the simplest reaction scheme (Fig. IB), the Km term contains the rate constant for conversion of substrate to product ( 23) If the rate of equilibrium is fast relative to k23, then Km approaches Kh. [Pg.33]

If we consider that the oxalate concentration is known the saturation curve (i.e. solution in the presence of solid calcium oxalate) is represented by the following equation obtained by using Eqs. (12.25), (12.22) (the solubility product), (12.18) (the value of k) and the concentration in oxalate species ( C204H + C204 ) ... [Pg.305]

A measure of photosynthetic efficiency and productivity can be obtained from the light-saturation curve of photosynthesis. This type of analysis is necessary and sufficient for the measurement of the vital signs of photosynthesis [Melis et al. 1999], In such measurements, the rate of O2 evolution, when plotted as a function of irradiance, first increases linearly and then levels off as the saturating irradiance (Is) is approached [Neale et al. 1993]. The slope of the... [Pg.122]

Another key variable in batch cooling is seeding. The difficulty is in determining the seed point, which is ideally when the batch temperature first crosses the saturation curve. However, this temperature can be affected by batch-to-batch variations in several factors, including the actual concentration of the material to be crystallized, as well as by impurities that can affect the solubility. If the seed is added at a temperature above the solubility temperature, some or all of it can dissolve, resulting in uncontrolled nucleation. If the seed is added at a temperature too far below saturation, the product may have already nucleated. In either case, the increase in nucleation could result in a decrease in impurity rejection and/or a change in particle size distribution and other physical attributes. [Pg.6]

Equation (46) assumes that the liquid is uniformly distributed in the agglomerate. The product can be calculated from the capillary pressure/saturation curve (Figure 64(b)). [Pg.95]

Figure 5. Saturation kinetics the dependence of enzyme catalysis on the concentration of substrate. Reaction velocity represents the rate at which product is formed. (A) shows a hyperbolic saturation curve for two hypothetical enzymes. One binds its substrate more tightly than the other and reaches saturation at lower substrate concentration. This enzyme has a lower value, the substrate concentration where the reaction is half of maximum. The other binds the substrate more loosely and reaches the same velocity but requires higher substrate concentrations. (B) shows hypothetical velocities for cooperative enzymes. Although more complex, these enzymes also show the phenomenon of saturation. Figure 5. Saturation kinetics the dependence of enzyme catalysis on the concentration of substrate. Reaction velocity represents the rate at which product is formed. (A) shows a hyperbolic saturation curve for two hypothetical enzymes. One binds its substrate more tightly than the other and reaches saturation at lower substrate concentration. This enzyme has a lower value, the substrate concentration where the reaction is half of maximum. The other binds the substrate more loosely and reaches the same velocity but requires higher substrate concentrations. (B) shows hypothetical velocities for cooperative enzymes. Although more complex, these enzymes also show the phenomenon of saturation.
The solutus curve, in binary SSAS systems with ideal or positive solid-solution free-energies of mixing and with large differences (more than an order of magnitude) in end-member solubility products, will closely follow the pure-phase saturation curve of the least soluble end-member (except at high aqueous activity fractions of the more soluble component, e . figure 1). In contrast, ideal solid-solutions with very close end-member solubility products (less than an order of magnitude apart) will have a solutus curve up to 2 times lower in EH than the pure end-member saturation curves. The factor of 2 is obtained for the case where the two end-member solubility products are equal and can be derived from equations 4, 16 and 17. [Pg.81]

In the presence of activator, pyruvate, the substrate saturation curves of the R. ruhrum ADP-Glc PPase are hyperbolic at low temperatures. Using kinetic studies its reaction mechanism was studied. The product inhibition patterns eliminated all known sequential mechanisms except the ordered BiBi or Theorell—Chance mechanisms. Small intercept effects suggested the existence of significant concentrations of central transis-tory complexes. Kinetic constants obtained in the study also favored the ordered BiBi mechanism. In addition studies using ATP-[ P]-pyrophosphate isotope exchange at equilibrium supported a sequential-ordered mechanism, which indicated that ATP is the first substrate to bind and that ADP-Glc is the last product to... [Pg.435]

Under conditions of low photorespiration, about 90% of photochemical product is allocated to COj fixation. The progression from light limitation to light saturation in photosynthesis is illustrated in Pig. 3 A which shows a typical light saturation curve for photosynthesis illustrated in the shmb Juanulloa aurantiaca. The quantum requirement per mole COj fixed (on an incident irradiance basis) increases as the irradiance and rate of CO2 assimilation increase. The higher the flux the lower the efficiency of COj assimilation (Fig. 3B). As the ATP and NADPH requirements for COj fixation are independent of... [Pg.311]

Enzymes can catalyze up to several million reactions per second. Enzyme rates depend on solution conditions and substrate concentration (Jayam et al., 2005]. The maximum speed of an enzymatic reaction is based on the substrate concentration until a constant rate of product formation. This is shown in Fig. 4.3 for indicating the saturation curve. Michaelis-Menten constant (/fm) is the substrate concentration required for an enzyme to reach... [Pg.144]

On PT diagrams the lines of constant composition are related to the saturation curves that appear on Fxy and Txy diagrams specifically, these three sets of saturation curves are related through a triple product rule. [Pg.383]


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See also in sourсe #XX -- [ Pg.184 ]




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Saturation curve

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