Abstract
Refolding of bovine serum albumin and its proteolytic fragments. Regain of disulfide bonds, secondary structure, and ligand-binding ability.
Highlights
Upon reduction of disulfide bonds and denaturation early proposal invoked a kinetically limited search of strucwith urea, ablumin (582 residues) and three fragments tures [5], an idea that was expanded to generatetestable showed loss of predictions withWetlaufer’ssuggestion [6] thatthe large their characteristic circulardichroism patterns and of globular domains often observed in single chain proteins are their binding ability for bilirubin, palmitate, and an- the resultof independent initiation angdrowth processes
Serum albuminis especially well suited to this type of investigation, because it is a single chain of 582 amino acids
We report on the rates of formation of disulfide bonds,of specific ligand-binding properties, and of the circular dichroism, as well as the antibody-combining ability upon refoIding of reduced forms of
Summary
(Received for publication, February 25, 1980, and in revised form, August 11, 1980). Kyung Oh JohansonS, Donald B. The fragments regained ligandbinding ability more rapidly than did albumin Taken together, these studies demonstrate independent folding of structural regions and support the concept of multiple sites fonrucleation and growth of native strucreadily upon oxidative refolding of two COOH-terminal fragments. We report on the rates of formation of disulfide bonds,of specific ligand-binding properties, and of the circular dichroism, as well as the antibody-combining ability upon refoIding of reduced forms of. Bilirubin solutions were prepared fresh daily in dilute NaOH, pH
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