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Properties of thiol-specific anti-oxidant protein or calpromotin in solution.

Abstract：

:We have isolated calpromotin, a protein reported abundant in human red cells and shown to be of significance for KCl transport. We show that calpromotin is identical to a radical scavenger protein, thiol-specific antioxidant protein (TSA). Calpromotin is known to exist partially as a large complex of identical subunits and partially as dimers probably held together by disulfide bridges. The stability of the high-molecular-weight form was studied by variations of pH and urea concentration. It is shown that the equilibrium between the large complex and the dimeric subunit is governed by the dissociation of a group with a pK value of about 7.5. Dissociation of the complex was also complete at 2.5 M urea, where no unfolding of the peptide chains was detectable.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kristensen P,Rasmussen DE,Kristensen BI

doi

10.1006/bbrc.1999.1107

subject

Has Abstract

pub_date

1999-08-19 00:00:00

pages

127-31

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(99)91107-5

journal_volume

262

pub_type

杂志文章

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