Preparation of Human Immunoglobulin Free of Plasmin and Anticomplement Activities
- 5 March 1977
- journal article
- research article
- Published by Wiley in Vox Sanguinis
- Vol. 32 (3), 143-158
- https://doi.org/10.1111/j.1423-0410.1977.tb00619.x
Abstract
Human Ig[immunoglobulin]G 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 (Cohn FII) 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 [poliovirus, cytomegalovirus and herpes simplex virus] 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.This publication has 27 references indexed in Scilit:
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