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 Citation Map 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 Lee, J. Y. Articles by Hirose, M. Search for Related Content PubMed PubMed Citation Articles by Lee, J. Y. Articles by Hirose, M. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 267, Issue 21, 14753-14758, Jul, 1992

Partially folded state of the disulfide-reduced form of human serum albumin as an intermediate for reversible denaturation

JY Lee and M Hirose
Research Institute for Food Science, Kyoto University, Japan.

The conformation of the fully disulfide-reduced state of human serum albumin was investigated by tryptophan fluorescence spectrum, CD analyses, and size-exclusion chromatography. Both the reduction of the native disulfide-bonded form under nondenaturing conditions and the refolding of the urea-denatured disulfide-reduced form under reduced conditions yielded almost exactly the same disulfide-reduced state with partially folded unique conformation that was clearly distinguished from either the native or fully denatured state. In addition, the interconversion between the urea-denatured reduced form and the partially folded reduced form was reversible with each other; by reoxidation, the partially folded reduced form was converted to the disulfide-bonded form. The conformation of disulfide-reduced serum albumin was highly variable depending on pH and ionic strength conditions. Thus, we concluded that the disulfide-reduced state with partially folded variable conformation is involved in the reversible interconversion between the denatured reduced form and the native disulfide-bonded form of human serum albumin.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				N. Tanaka, Y. Tani, H. Hattori, T. Tada, and S. Kunugi Interaction of the N-terminal domain of Escherichia coli heat-shock protein ClpB and protein aggregates during chaperone activity Protein Sci., December 1, 2004; 13(12): 3214 - 3221. [Abstract] [Full Text] [PDF]

				M. Onda and M. Hirose Refolding Mechanism of Ovalbumin: INVESTIGATION BY USING A STARTING UREA-DENATURED DISULFIDE ISOMER WITH MISPAIRED CYS367-CYS382 J. Biol. Chem., June 20, 2003; 278(26): 23600 - 23609. [Abstract] [Full Text] [PDF]

				M. Dockal, D. C. Carter, and F. Ruker Conformational Transitions of the Three Recombinant Domains of Human Serum Albumin Depending on pH J. Biol. Chem., February 4, 2000; 275(5): 3042 - 3050. [Abstract] [Full Text] [PDF]

				M. Dockal, D. C. Carter, and F. Ruker The Three Recombinant Domains of Human Serum Albumin. STRUCTURAL CHARACTERIZATION AND LIGAND BINDING PROPERTIES J. Biol. Chem., October 8, 1999; 274(41): 29303 - 29310. [Abstract] [Full Text] [PDF]

				J. Ren, K. Kachel, H. Kim, S. E. Malenbaum, R. J. Collier, and E. London Interaction of Diphtheria Toxin T Domain with Molten Globule-Like Proteins and Its Implications for Translocation Science, May 7, 1999; 284(5416): 955 - 957. [Abstract] [Full Text]

				M. Onda, E. Tatsumi, N. Takahashi, and M. Hirose Refolding Process of Ovalbumin from Urea-denatured State. EVIDENCE FOR THE INVOLVEMENT OF NONPRODUCTIVE SIDE CHAIN INTERACTIONS IN AN EARLY INTERMEDIATE J. Biol. Chem., February 14, 1997; 272(7): 3973 - 3979. [Abstract] [Full Text] [PDF]