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- W2089483876 abstract "Cleavage of a human IgG cryoglobulin (6·5 S, γ 1:λ, Gm factor 4) into its constituent L and H chains could only be accomplished in the presence of mercaptoethanol. Dissociation of Dv cryoglobulin could not be affected by structure-diruptive solutes like urea (8 M ) and guanidineHCl (6 M ). The weight-average apparent mol. wt as determined by sedimentation equilibrium analysis were 50,500 ± 1000 and 26,000 ± 1000 for H and L chains of Dv cryoglobulin, respectively. Sedimentation velocity analysis showed the self-association of the H chains, depending on the solvent environment. The reduced-aminoethylated H chains of Dv cryoglobulin exhibited visible cryo-gel formation and under identical experimental conditions, the L chains remained in solution. These studies indicate that the sites responsible for self-association leading to cryo-gel formation are located on the H chains which show a higher degree of resiliency after being with strong protein denaturants." @default.
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- W2089483876 date "1974-11-01" @default.
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- W2089483876 title "Studies on cryoprecipitation: Covalent structure of a human IgG cryoglobulin and its gelation characteristics" @default.
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- W2089483876 doi "https://doi.org/10.1016/0019-2791(74)90270-5" @default.
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