Abstract
We have recently demonstrated that sex-limited protein (Slp) plays a key role in an EDTA-resistant mouse complement activation pathway. A rapid procedure, utilizing classical chromatography methods on an FPLC system, was developed for the isolation of functionally active Slp. The method is based on the fractionated precipitation of serum by polyethylene glycol 6000, followed by heparin Sepharose Cl-6B affinity chromatography, Mono Q anion exchange and Superose 12 gel filtration. The isolation of Slp was monitored by a hemolytic assay. The procedure resulted in the purification of Slp, which by SDS-PAGE gave a single band of M r 200,000 under non-reducing conditions, and under reducing conditions three bands corresponding to M rs of 105,000, 76,000 and 37,000.
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