Weight, vs. mass

Cumulative leaching plots (cumulative mass of element leached per mass dry weight of ash vs. cumulative mass of leachate collected vs. mass dry weight of ash) for Pb, Cu, and Zn are shown in Fig. 12. The plots are constructed using measured element leachate concentrations and volumes of leachate collected. In many cases, the detection limit of the element was used as the concentration, so that the traces are conservative. Over time, the pH of leachates has dropped from about 12 to about 9. Data for Cd are not shown because of the high number of detection limit values that were observed in both the unamended and amended lysimeters. 

The molar mass distributiMi for two polymers. The first polymer (continuous trace) follows the Flory-Schulz MMD with Mn = 40000 Mw is the double, i.e., Mw = 80000). The second polymer (dotted trace) follows the Schulz-Zimm MMD with Mn = 40000 and Mw = 120000. The molar mass distribution is diplayed as the molar fraction (a) and weight fraction (b) vs. mass. 

If we do that (Problem 6.9) we find analogs to most of the equations and procedures shown in this chapter, with partial molar properties replaced by those same properties divided by the molecular weight. Such properties have no common name perhaps they are best called partial mass properties. The most commonly seen application is with plots of enthalpy per unit mass vs. mass fraction, as shown for water and sulfuric acid in Figure 6.8. As shown in Problem 6.9, if we apply the method of tangent intercepts to this figure, the intercept values are the partial mass enthalpies. 

The actual variation of the mass with time is on the left of the figure. After a brief induction time, the mass drops linearly with time, often until 90 percent or more of the water has evaporated. It then drops at a slower rate. This linear drop is the norm and is strikingly accurate to test it for yourself, just hang a wet tee shirt on a lab balance and record the weight vs. time. 

The molecular masses of heme catalases are usually significantly higher as compared with peroxidases. If expressed in Lg-1s-1, rate constants for the Fem-TAML activators when compared with catalase from beef liver, which has a molecular weight 250,000 gmol-1 (Table IV, entry 13) (89), look very impressive, viz. 17 L g 1 s-1 for 11 vs. 22 L g 1 s 1 for the enzyme. Nevertheless, the catalase-like activity of the Fem-TAML activators can be suppressed by the addition of electron donors -it is negligible in the presence of the substrates tested in this work. In Nature, catalases display only minor peroxidase-like activity (79) because electron donors bulkier than H202 cannot access the deeply buried active sites of these massive enzymes (90). The comparatively unprotected Fem-TAML active sites are directly exposed to electron donors such that the overall behavior is determined by the inherent relative reactivity of the substrates. 

Fig. 3 SDS-PAGE Photograph Separation (Lane Mr and A) and activity staining (Lane B and C) of the crude filtrate of Funalia trogii. Lane Mr standard molecular weight markers ([3-galactosi-dase, 118.0 kDa bovine serum albumin, 79.0 kDa ovalbumin, 47.0 kDa carbonic anhydrase, 33.0 kDa P-lactoglobulin, 25.0 kDa and lysozyme, 19.5 kDa). Relative mobilities of the standard markers vs. common logarithms of their molecular masses were plotted.With the linear regression output, the molecular masses of the proteins in the crude filtrate were estimated (taken from [18])...

B. Mass fraction (or weight percent) retained (oversize) vs. average particle diameter... 

C. Cumulative mass fraction (or weight percent) (undersize) through each screen vs. average screen opening... 

Figure 1. Top portion shows a plot of the observed Fenvalerate response vs. the mass (ng). Lower plot gives ordered, normalized residuals from the fit of model-3 to the data (Table IV) using the weights given in Table III. (Symbols indicate the five replicates, and the plotted residuals are normalized by the standard deviations for these individual replicates. The "goodness of fit residuals of the model to the means of the replicates are larger by 1/5T because they are normalized by the standard errors at each concentration.)...

Depending on the selected polymerization reaction, the polymerization conditions, and potential side reactions one may obtain different molar mass distributions - even if only one single type of monomer is polymerized. As an example, Fig. 2.11 shows the plot of the overall masses w, (w = weight) of all macromolecules i in the sample vs. their respective molecular weights M, ... 

The mass of internal standards and analytes of interest in each sample are determined from the appropriate standard curves (mass vs. AUC). The total mass of excreted cholesterol and related sterols is calculated from the 5a-cholestane peak (i.s.) in each sample sterol mass per 0.5 g feces = sterol massGC x 40/i.s. masscc- The total excreted per 3 days is then calculated from the total fecal mass collected. Data are finally reported as mass (or moles) excreted per day per gram body weight. 

Fig. 33 Double logarithmic plots of weight average molar mass (Mw) vs. average hydro-dynamic radius (i h> for the HPAM5 chains in the presence of different amounts of Ca++ ions [130]...

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