Physical Principles and Techniques of Protein ChemistryPhysical Principles and Techniques of Protein Chemistry Part C ... |
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Page 160
For measurements at extremes of pH , the volume of reagent added is significant
, and the absorption values must be corrected for dilution . The same volume of
water or buffer must also be added to the reference solution before measuring
the ...
For measurements at extremes of pH , the volume of reagent added is significant
, and the absorption values must be corrected for dilution . The same volume of
water or buffer must also be added to the reference solution before measuring
the ...
Page 436
Electrophoresis was carried out in either phosphate buffer ( pH 6 . 1 , ionic
strength 0 . 043 ) , or a phosphate - borate buffer of about the same pH and ionic
strength . The zone patterns are presented in Figs . 26a and 26b ; whereas the
protein ...
Electrophoresis was carried out in either phosphate buffer ( pH 6 . 1 , ionic
strength 0 . 043 ) , or a phosphate - borate buffer of about the same pH and ionic
strength . The zone patterns are presented in Figs . 26a and 26b ; whereas the
protein ...
Page 439
Examples of protein - buffer interactions have been presented above for
carboxylate , phosphate - borate , borate , and tris - borate buffers . There is also
ample evidence for multiple electrophoretic peaks generated by interaction with
solvents ...
Examples of protein - buffer interactions have been presented above for
carboxylate , phosphate - borate , borate , and tris - borate buffers . There is also
ample evidence for multiple electrophoretic peaks generated by interaction with
solvents ...
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Contents
The Enhancement of Contrast | 21 |
The Preservation of Specimens | 35 |
Examples of the Application of Electron Microscopy to the Study | 48 |
Copyright | |
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Common terms and phrases
absorbance absorption acid appears applied atoms axis binding birefringence boundary buffer calculated cell charge Chem chromophores complex concentration constant containing contrast corrected corresponding curve decrease dependence determined dielectric difference diffusion dipole direction discussed distribution effect electric electric field electron electrophoresis emission energy equation equilibrium example excitation experimental experiments factor fluorescence fraction frequency function given groups Herskovits important increase indicates intensity interactions ionic ions length light limited macromolecules measured method mobility molecular molecules observed obtained occurs optical orientation particles patterns peaks perturbation phase phenolic polarization position possible preparation present produced protein quantum range ratio reaction reference relative relaxation respectively rotation sample separation serum albumin shift shown single solution solvent specimen spectra spectrum strength structure studies technique temperature theory tion transfer transition tryptophan unit usually volume wavelength yield zone