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• W2007794678 abstract "Human secretory component (SC) was isolated from human whey by affinity chromatrography on IgM-Sepharose adsorbents. Human IgM monoclonal proteins were isolated from sera of patients with Wladenstrom's macroglobulinemia by repeated euglobin precipitation. Sepharose 4B was activated with CNBr and covalently coupled to the isolated IgM protein. When was diluted 1:10 in 0.01 M citrate, 0.02 M phosphate, pH 6.8, containing a final concentration of 0.25 mg Fe(NH4)2 SO4/ml of diluted whey, Dilution of whey in iron-containing buffer was found to suppress the binding of lactoferrin to IgM-Sepharose. The IgM-Sepharose was incubated for 2 hr at 4°C with diluted whey (0.2–0.5 ml Sepharose IgM/ml of neat whey), following which the mixture was poured into a chromatographic column and washed extensively with phosphate buffered saline (PBS) to remove unadsorbed protein. The adsorbed protein was eluted with 1.10 M KSCN, 0.01 M potassium phosphate pH 6.8–7.0, dialysed against PBS and fultered on Sephadex G-200 column. Two peaks were obtained, the second containing SC. The purified SC gave a single major band on polyacrylamide SDS electrophoresis, on arc in immunoelectrophoresis, and was shown to bind to IgM and polymeric IgA with the same relative affinity as conventionally purified SC. The yield obtained was 250–300 mg SC/1 whey (i.e. ⋍ 70% theoretical), and was approx 3–10 times greater than that obtained by conventional methods." @default.
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• W2007794678 date "1977-02-01" @default.
• W2007794678 modified "2023-09-27" @default.
• W2007794678 title "Isolation of human secretory component by affinity chromatography on IgM-Sepharose" @default.
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• W2007794678 doi "https://doi.org/10.1016/0019-2791(77)90289-0" @default.
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