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Purification of the Human Complement Protein Clq by Affinity Chromatography¹

From the Departments of Microbiology and Public Health, and Human Development, Michigan State University, East Lansing, Michigan 48823

Abstract

A subunit of the first component of human complement C1q, was purified by the technique of affinity chromatography. The chromatographic resin was cyanogen bromide-activated Sepharose covalently linked to human IgG. For the removal of traces of IgM it was necessary to subject further the C1q obtained from the chromatographic step to ultracentrifugation in sucrose gradients. The highly purified C1q was characterized immunochemically and according to its electrophoretic mobility in polyacrylamide gel. The purified material was capable of combining with C1r and C1s to reconstitute fully active macromolecular C1.

Footnotes

¹ This work was supported by Public Health Service Pre-doctoral Training Grant GM 01911-04 and Public Health Service Grant 1-ROI-AM-13679-03 from the National Institutes of Health. This is Journal Article No. 5935 from the Michigan Agricultural Experiment Station.

² Present address: Biology Department, California Institute of Technology, Pasadena, California 91109.

³ Recipient National Institutes of Health. Career Development Award No. 1-K4-AM-70,340-01.