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• W2023371279 abstract "Beta-2 microglobulin (β2M) is a 12,000 dalton protein associated with membrane-bound cell surface antigens. Variants of β2M, β2MA and β2MB, were first detected by Michaelson et al. (Immuno- genetics11, 93–95, 1980). An improved method was used to purify β2MA and β2MB from BALB/c and C57BL/6 mouse livers, respectively. Reproducible yields of 10% were obtained. The purifications were accomplished by a 3 M sodium thiocyanate (NaSCN) extraction of a crude membrane fraction, an acid precipitation step, gel filtration on Sephadex G-75 and ion-exchange chromatography on DEAE-cellulose and CM-cellulose in that order. The elution profile of β2MA and β2MB on the ion-exchange columns was found to be different, indicating the presence of structural changes. β2MA was found to be more acidic (pI = 7.35) than β2MB (pI = 7.68) by isoelectric focusing in gels. Complete sequence analysis of β2MA and partial sequence analysis of β2MB (61 of 99 residues) were performed by automated Edman degradation of the intact chain and of the overlapping peptides obtained by: (a) tryptic cleavage at arginines after acetimidation of lysine side chains, (b) BNPS-skatole cleavage at trytophan residues and (c) hydroxylamine cleavage at asparagine-glycine linkages. A comparison of the primary structure of β2MA to the partial amino acid sequence obtained for β2MB revealed a single amino acid substitution (aspartic acid for alanine at position 85) that accounts for the differences in biochemical properties observed." @default.
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• W2023371279 date "1982-03-01" @default.
• W2023371279 modified "2023-10-16" @default.
• W2023371279 title "Purification and characterization of mouse beta-2 microglobulin: Allelic variants from two different strains" @default.
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• W2023371279 doi "https://doi.org/10.1016/0161-5890(82)90209-7" @default.
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