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Protein iodinated, titration curves

The reaction of iodine with proteins is neither quantitative nor completely specific, and since it may be expected to result in chemical substitution or oxidation of a variety of groups the interpretation of the titration curve of an iodinated protein is subject to considerable uncertainty. At-... [Pg.169]

The titration curves of native and iodinated insulins are compared in Fig. 137. The two curves differ by essentially four groups in the tyrosyl ionization region. A discussion of the departure from four, and the analytical data indicating that the four tyrosyl groups were completely iodinated without any other alteration in the protein, have been presented elsewhere (Gruen et al., 1959a). [Pg.250]

Fia. 137. Titration curves at 25°C. of zinc-free insulin, , and of iodinated insulin, O, in 0.3 M KCl, showing the difference, Ar, in the number of groups titrated in the region of diiodotyrosyl and tyrosyl ionization. The zero for the r-scale is arbitrary. The protein was partially insoluble in the region to the left of the vertical bar on each curve (Gruen et al., 1959a). [Pg.251]

Iodination of proteins has produced measurable changes in the titration curves. In zein (280), insulin (125), and pepsin (6) the region of the titration curves usually assigned to the phenolic group of tyrosine (pK=10) is displaced in iodinated proteins in the direction of increased acidity by nearly 2 pH units. This is apparently not true for iodinated globin (299). [Pg.208]


See other pages where Protein iodinated, titration curves is mentioned: [Pg.170]    [Pg.208]   
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