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Human IgG separated by Cohn fractionation showed variability in the content of aggregates, plasminogen and anticomplement activity. The plasminogen was removed or markedly reduced by affinity chromatography on Sepharose-lysine. Anticomplement activity was reduced by chromatography of Cohn fraction II on DEAE-cellulose. Preparations of IgG obtained by chromatography of intermediates from Cohn fractionation (e.g. Cohn FII + FIII or FII + FIII W) on DEAE-cellulose were devoid of aggregates, plasminogen and exhibited reduced anticomplement activity. The initial levels of specific antibody activity to viral agents were recovered in the IgG fractions. Fragmentation of IgG during storage was prevented or greatly reduced by removal of plasminogen by affinity chromatography on Sepharose-lysine.
A F Habeeb, and
R D Francis
February 1983,
Japanese journal of medical science & biology,
A F Habeeb, and
R D Francis
January 1982,
Vox sanguinis,
A F Habeeb, and
R D Francis
January 1961,
Zeitschrift fur Hygiene und Infektionskrankheiten; medizinische Mikrobiologie, Immunologie und Virologie,
A F Habeeb, and
R D Francis
July 1960,
Vox sanguinis,
A F Habeeb, and
R D Francis
June 1987,
Zhurnal mikrobiologii, epidemiologii i immunobiologii,
A F Habeeb, and
R D Francis
April 1964,
Thrombosis et diathesis haemorrhagica,
A F Habeeb, and
R D Francis
January 1978,
International archives of allergy and applied immunology,
A F Habeeb, and
R D Francis
July 2012,
Natural product communications,
A F Habeeb, and
R D Francis
April 1986,
Gematologiia i transfuziologiia,
A F Habeeb, and
R D Francis
January 1976,
Medycyna doswiadczalna i mikrobiologia,
