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Chromatographic purification of ySmCL1 on gel filtration and anion-exchange matrices. Ten to 20 μg of protein of concentrated culture medium (lane 1), S200 HR peak II (lane 2), and QAE-Sephadex run-through pool I (lane 3), pool II (lane 4), and pool III (lane 5) were separated by SDS-PAGE (12% gel) under reducing conditions. Gels were either stained with Coomassie brilliant blue R (A) or transferred to nitrocellulose and probed with rabbit anti-bSmCL1 serum (B) or control serum (C).
