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PURIFICATION FROM EUGLOBULIN OF THE FIRST COMPONENT (Cl) OF COMPLEMENT AND ITS SUBCOMPONENTS BY HEPARIN‐SEPHAROSE CHROMATOGRAPHY
Author(s) -
Zeipel G.,
Hanson HannaStina,
Stedingk L.V.
Publication year - 1977
Publication title -
acta pathologica microbiologica scandinavica section c immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0304-1328
DOI - 10.1111/j.1699-0463.1977.tb03621.x
Subject(s) - chemistry , ionic strength , heparin , chromatography , adsorption , sepharose , sephadex , affinity chromatography , ionic bonding , elution , biochemistry , enzyme , ion , organic chemistry , aqueous solution
Most of the CI material of euglobulin was adsorbed to heparin‐Sepharose at an ionic strength of 0.265. After desorbtion at an ionic strength of 0.415 the CI material was found to be purified six to seven‐fold. Highly purified subcomponents C1q, CIr and CIs were recovered at DEAE‐Sephadex chromatography from such purified CI material after EDTA‐treatment. Tests on isolated C1q, CIr and CIs disclosed in addition to the wellknown interaction between heparin and C1q an equally strong or even stronger interaction between heparin and CIs. Even CIr was adsorbed to heparin although by somewhat weaker ionic bonds.