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Properties of thyroglobulin. XII. Comparison of the configurational states of reduced and unreduced thyroglobulin
Author(s) -
Edelhoch H.,
Steiner R. F.
Publication year - 1966
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1966.360040905
Subject(s) - thyroglobulin , chemistry , guanidine , urea , viscosity , biophysics , inorganic chemistry , chromatography , biochemistry , thermodynamics , thyroid , endocrinology , physics , medicine , biology
The relaxation time of thyroglobulin has been determined in water at. neutral pH, in concentrated urea and guanidine solutions, at alkaline pH, both before and after reduction with β‐mercaptoethanol. The structure of thyroglobulin in concentrated urea solutions is markedly affected by the pH, Time‐dependent changes occur in thyroglobulin in concentrated urea or guanidine solutions which arc observable by polarization of fluorescence but not by optical rotation or viscosity. The reduction of the disulfide crosslinks of thyroglobulin in urea at high pH or in guanidine produces linear polypeptide chains with few if any permanent contacts between segments.