Purification and characterization of human serum C-reactive protein.

Abstract:

:A simple and rapid purification method for human serum C-reactive protein (CRP) was developed. CRP was strongly adsorbed on a DEAE-cellulose column and was easily separated from other serum proteins. CRP was purified approximately 1,000-fold with a high yield (50%). The final preparation showed a single band as judged by SDS-polyacrylamide gel electrophoresis, polyacrylamide gel disc electrophoresis, and polyacrylamide gel isoelectric focusing. The fluorescence of the complex of CRP and 8-anilino-1-naphthalene sulfonate (ANS) changed with change of the pH, suggesting that CRP may show pH-dependent conformational change. This finding could account for the peculiar behavior of the protein in isoelectric focusing; it shows an isoelectric point of 7.4 when the starting pH is 7.0, whereas it shows two isoelectric points, 5.3 and 7.4, when the starting pH is 5.5. Ca2+-dependent change of the fluorescence of the complex of CRP and ANS was also detected. These results suggest a pH- and Ca2+-dependent conformational change of CRP.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Tsujimoto M,Inoue K,Nojima S

doi

10.1093/oxfordjournals.jbchem.a134483

subject

Has Abstract

pub_date

1983-11-01 00:00:00

pages

1367-73

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

94

pub_type

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