Physical Principles and Techniques of Protein ChemistrySydney J. Leach Physical Principles and Techniques of Protein Chemistry Part C ... |
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Page 151
... solution must be used as a reference solution . There is one serious disadvantage of the method when used for tyrosine analysis . The absorption of ... solution . The use of 3. ULTRAVIOLET ABSORPTION 151 Determination in Acid Solution.
... solution must be used as a reference solution . There is one serious disadvantage of the method when used for tyrosine analysis . The absorption of ... solution . The use of 3. ULTRAVIOLET ABSORPTION 151 Determination in Acid Solution.
Page 160
... solution can often be conveniently altered by adding concentrated acid or base solution to the sample solution using a syringe microburet or a glass rod drawn to a fine tip . Except at ex- tremes of pH , the volume change so produced is ...
... solution can often be conveniently altered by adding concentrated acid or base solution to the sample solution using a syringe microburet or a glass rod drawn to a fine tip . Except at ex- tremes of pH , the volume change so produced is ...
Page 161
... Solutions For convenience , the reference solution for spectrophotometric titra- tions should have all the titratable chromophores in one absorbing form ( see Section IV ) . For titrations of phenolic groups , a neutral pH reference ...
... Solutions For convenience , the reference solution for spectrophotometric titra- tions should have all the titratable chromophores in one absorbing form ( see Section IV ) . For titrations of phenolic groups , a neutral pH reference ...
Contents
Electron Microscopy | 2 |
Ultraviolet Absorption | 3 |
Dielectric Properties of Proteins | 7 |
Copyright | |
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absorption absorption spectrum amino acids applied atoms axis Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Cann cell Chem chromophores coefficient components concentration curve Debye denaturation density determined dielectric constant dielectric increment dielectric relaxation difference spectrum dipole moment Edelhoch effects electric birefringence electric field electron microscope electrophoresis elution volume emission enzyme equation equilibrium excitation experimental film fluorescence fraction frequency gel filtration gradient groups instrument intensity interactions ionic strength ions lens light linear macromolecules magnification measured method micrographs migration mobility molar molecular weight molecules moving-boundary observed obtained optical ovalbumin parameter particles peaks permanent dipole perturbation phase phenolic photomultiplier Phys plot polarization polymer produced protein quantum yield ratio reaction relaxation residues resolution resolving power ribonuclease scattering shadow shown in Fig solution solvent specimen spectra structure studies technique temperature theoretical theory tion tryptophan tyrosine values wavelength Weber Winzor zone