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- W2017679111 abstract "A simple technique is described to remove traces of concanavalin A (Con A) from human α-1-antitrypsin (α-1-AT) purified on commercially available Con A-Sepharose. The α-1-AT was fractionated from serum by ammonium sulfate precipitation followed by chromatography on DEAE-cellulose, Con A-Sepharose, and activated thiol-Sepharose at 4°C with solution pH ranges of 7.4–7.6 in all steps. Contaminating Con A was easily removed by binding α-1-AT through the reactive sulfhydryl group to the activated thiol-Sepharose gel and washing away the contaminating Con A with a solution of methyl-α-d-glucopyranoside before final elution of bound α-1-AT. This simple procedure yields purified α-1-AT free of traces of Con A. The α-1-AT was obtained in overall yields of 40–48% from serum with an average molecular weight of 53,500 ± 3000 determined on 15% disc polyacrylamide gels containing sodium dodecyl sulfate (SDS). The isolated α-1-AT exhibited unaltered Pi M phenotype compared to serum α-1-AT but contained traces of several other serum proteins." @default.
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- W2017679111 date "1979-01-01" @default.
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- W2017679111 title "Preparation of concanavalin a free purified α-1-antitrypsin" @default.
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- W2017679111 doi "https://doi.org/10.1016/s0003-2697(79)80134-7" @default.
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