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- Abbreviations used: Con A, concanavalin A; α2M, α2-macroglobulin; SDS, sodium dodecylsulfate; PAGE, polyacrylamide gel electrophoresis
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- Hereafter referred to as 50% and 70% ammonium sulfate fractions
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- Electrostatic interaction was excluded as a possibility since this type of complex, between oppositely charged protein pairs, occurs at low ionic strength and results in insolubility. Dissociation of these complexes occurs as the ionic strength is increased34–36 The albumin-IgA and -IgG complexes were stable in 0.14 M NaCl (Fig. 1) and also in 1.0 M NaCl (Table I, Fig. 5). The disulfide nature of the interaction is also supported by the fact that the complexes were stable in the presence of SDS (100o C for 5 min) but were readily dissociated in SDS-2-mercapto-ethanol under the same conditions (Fig. 7)
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