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Results for Individual Proteins

Titration curves for bovine a-chymotrypsinogen have been determined under a variety of conditions by Wilcox (1961). The results are summarized in Table IX. The spectrophotometric titration of the phenolic groups is shown in Fig. 4. [Pg.131]

It is seen that all four phenolic groups are titrated together in 6.4 M urea, whereas only two are titrated in the native protein. Even these two have sufficiently different pK s so that the titration of one is essentially complete before that of the second has begun. [Pg.131]

The count of side-chain amino groups corresponds to the analytical figure for lysine side chains in a denaturing solvent (8 Af urea). In the native protein, however, three of the thirteen lysine groups cannot be observed to titrate. The maximum positive proton charge ( S W ) is however the same in the native and denatured states, within the uncertainty of about [Pg.131]

More phenolic and amino groups are titrated slowly above pH 12 as the protein becomes denatured. [Pg.132]

The titration curve of native chymotrypsinogen is reversible between pH 2.5 and pH 11. Analysis by the methods of Section VI shows that the neutral pH region can be described by a single intrinsic dissociation constant for all three groups which titrate in the region, together with a w [Pg.132]


From this point of view, titration curves do not represent just another way of physically characterizing a protein molecule. More than most other physicochemical methods which are in common use, titration studies tend to emphasize individual differences among proteins, and this is reflected in the organization of this paper. There is a large section, entitled Results for Individual Proteins, which contains the many features of... [Pg.70]


See other pages where Results for Individual Proteins is mentioned: [Pg.69]    [Pg.131]    [Pg.99]   


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