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Method, Acker

Tray-by-Tray Calculation—Ackers and Wade Method... [Pg.92]

Van Acker, J. and Jones, D. (2002). Test methods for modified wood The EU-themahc network approach. International Research Group on Wood Preservation, Doc. No. IRGAVP 02-20255. [Pg.229]

Steere, R. E., and G. K. Ackers Restricted diffusion chromatography through calibrated columns of granulated agar gel a simple method for particle-size determination. Nature /9d, 475 76 (1962). [Pg.39]

Figure 3. Gel permeation data for linear randomly coiled polypeptides on various agarose resins, plotted according to the method of Ackers (9). M0 555 is plotted vs. the inverse error function complement of Kd (erfc 1 Kd). Lines drawn through the data points represent best fits obtained from linear least-squares analysis of the data. Numerical designation of each curve represents the percent agarose composition for the resin used. Filled triangles on the curve for the 6% resin, and the filled squares on the curve for the 10% resin are points determined using fluorescent proteins. Data for the labeled polypeptides were not included in the least-squares analysis. Figure 3. Gel permeation data for linear randomly coiled polypeptides on various agarose resins, plotted according to the method of Ackers (9). M0 555 is plotted vs. the inverse error function complement of Kd (erfc 1 Kd). Lines drawn through the data points represent best fits obtained from linear least-squares analysis of the data. Numerical designation of each curve represents the percent agarose composition for the resin used. Filled triangles on the curve for the 6% resin, and the filled squares on the curve for the 10% resin are points determined using fluorescent proteins. Data for the labeled polypeptides were not included in the least-squares analysis.
While the calibration curves presented in Figure 1 provide an adequate treatment of gel permeation calibration data, they are nonlinear in the extremes of the useful calibration regions. Two methods of data treatment may be used to provide linear representations of gel filtration results. These methods substantially increase the usefulness of the technique. The equations for these methods, developed by Porath (8) and Ackers (9), are as follows ... [Pg.322]

G. Ackers, Methods Enzymol. 27, 441-455 (1973), Academic Press (New York). Studies of protein ligand binding by gel filtration techniques. [Pg.255]

Indirect methods for obtaining information on the kinetics of the associa-tion/dissociation equilibrium include sedimentation velocity and GPC experiments. The application of these techniques is based on comparison of sedimentation or GPC elution curves with model curves based on theories for separation of unimers and micelles during a sedimentation velocity (Gilbert 1955) or GPC (Ackers and Thompson 1965 Coll 1971 Prochazka et at. 1988, 1989) experiment. Experiments have been performed that demonstrate several of the qualitative model predictions (Prochazka et at. 1989). The main conclusions were that GPC curves with two well-separated peaks can only result from a slow dynamic molecule micelle equilibrium, and that no simple interpretation of elution curves in terms of relative concentrations of unimer and micelles is possible (Prochazka et at. 1989). Thus no quantitative information on the kinetics of the molecule micelle equilibrium can be obtained from sedimentation velocity or GPC data. [Pg.198]

Lumry, R. (1995) On the interpretation of data from isothermal processes, in Johnson, M. and Ackers (eds.), Methods in Enzymology 259, Energetics of Biological Macromolecules, Acad. Press, San-Diego, pp. [Pg.210]

Ackers GK, Holt JM, Burgie ES, Yarian CS. Analyzing intermediate state cooperativity in hemoglobin. In Methods in Enzymology. [Pg.689]

ACK94] VAN ACKER K., DE BUYSER L., CELIS IP., VAN HOUTTE P., Characterization of thin nickel electrocoatings by the low incident beam angle diffraction method , J. Appl. Cryst, vol. 27, p. 56-66, 1994. [Pg.319]

Ackers GK, Johnson ML (editors), Methods in Enzymology, volume 295 Energetics of biological molecules. [Pg.223]

Figure 2. Schematic presentation of the method of Brumbauch and Ackers. Li t absorption is measured through a gel column (A5) and it is compared with that of free solution above the gel bed (A,). Vg represents the volume taken by the gel matrix. Figure 2. Schematic presentation of the method of Brumbauch and Ackers. Li t absorption is measured through a gel column (A5) and it is compared with that of free solution above the gel bed (A,). Vg represents the volume taken by the gel matrix.
Figure 3. Hypothetical column for the method of Brumbaugh and Ackers. Aj and A j repre-sent absorbances measured through equilibrated gel column (see Fig. 2). As shown, total ligand content is different in equal segments Aj (L 4) and At> (L = 3). For other details, see the text. Figure 3. Hypothetical column for the method of Brumbaugh and Ackers. Aj and A j repre-sent absorbances measured through equilibrated gel column (see Fig. 2). As shown, total ligand content is different in equal segments Aj (L 4) and At> (L = 3). For other details, see the text.
Ackers because of rapidity (ref. 35) and of potentially better accuracy. Binding constants from the recycling method roughly agreed with those obtained by other methods (ref. 35, 36). [Pg.356]

G. K. Ackers, in H. Neurath and R. L. Hill (Eds.), The Proteins, 3rd edn., Molecular Sieve Methods of Analysis, Academic Press, New York,... [Pg.396]

R. Valdes, Jr. and G. K. Ackers, in C.H.W. Hirs and S.N. Tlmasheff (Eds.), Methods in Enzymology, Vol. 61, Study of Protein Subunit Association Equilibria by Elution Gel Chromatography, Academic Press,... [Pg.396]

Under certain conditions, however, the micropores may be closed or reduced in size so that the BET nitrogen adsorption method measures only the exterior surface of the microgel particles. Such a product may thus have a low specific area especially when the process is conducted hot and the precipitate aged at High pH, as done by Acker and Winyall (424). [Pg.561]

E. Barbar and M. Hare, Characterization of the Cargo Attachment Complex of Cytoplasmic Dynein Using NMR and Mass Spectrometry , in Methods in Enzymology, eds. J. Holt, M. Johnson and G. Ackers, Elsevier, 2004, vol. 380, Energetics of Biological Macromolecules, Part E, p. 219. [Pg.28]


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See also in sourсe #XX -- [ Pg.316 ]




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