HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by de Crombrugghe, B. Articles by Edelhoch, H. Search for Related Content PubMed PubMed Citation Articles by de Crombrugghe, B. Articles by Edelhoch, H. Social Bookmarking                      What's this?

The Properties of Thyroglobulin

XI. THE REDUCTION OF THE DISULFIDE BONDS

From the ¹ From the Clinical Endocrinology Branch, National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, Bethesda, Maryland 20014

The extent of reduction of the disulfide groups in thyroglobulin by ß-mercaptoethanol has been investigated as a function of pH in aqueous media and in 8 m urea.

The products of reduction of thyroglobulin in dilute urea and in concentrated urea and guanidine solutions have been characterized by sedimentation and viscosity.

Cleavage of a few disulfide bonds produces a smaller molecule of the same molecular weight as that obtained by quantitative reduction of all the bonds.

On reduction in 5m guanidine, the 12 S subunit of thyroglobulin of million molecular weight is cleaved into two equal or similar sized molecules.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				W. B. Jakoby, L. Labaw, H. Edelhoch, I. Pastan, and J. E. Rall Thyroglobulin: Evidence for Crystallization and Association Science, September 30, 1966; 153(3744): 1671 - 1672. [Abstract] [PDF]