Premium
Purification of human C‐reactive protein by barium sulfate and preparative agarose electrophoresis
Author(s) -
KINDMARK CLAESOTTO L.,
WILLIAMS JIM C.
Publication year - 1989
Publication title -
apmis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0903-4641
DOI - 10.1111/j.1699-0463.1989.tb00494.x
Subject(s) - agarose , chemistry , chromatography , electrophoresis , agarose gel electrophoresis , gel electrophoresis , molecular weight size marker , affinity chromatography , polyacrylamide gel electrophoresis , gel electrophoresis of proteins , biochemistry , enzyme , dna
A procedure is described for the purification of C‐reactive protein (CRP) from human serum. The methods described take advantage of the barium sulfate adsorption property of CRP and the unique biophysical property of CRP migration during electrophoresis in agarose gels containing Ca 2+ . The purified CRP had an apparant molecular weight of 28,000 as determined by migration of the reduced protein during SDS polyacrylamide gel electrophoresis. The described procedure has the advantage of not requiring either molecular sieve or affinity chromatography for purification of homogenous CRP from human sera.