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• W1993627674 abstract "Sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the immunoblotting technique, were applied to structural analysis of a single protein (alpha-2-macroglobulin, α-2-M) in human serum or plasma without prior purification of this protein. The use of immunoglobulin fractions of four monospecific polyclonal antibody preparations to α-2-M in the immunoblotting step showed marked unspecific binding to the proteins fixed onto nitrocellulose. Immunospecific purification of the antibodies by two different methods, and the introduction of biotinylated antibodies and avidin-peroxidase, removed the background binding. When reduced proteins were fixed onto nitrocellulose a quantitative loss of α-2-M antigen reactivity was observed, compared to identical nonreduced samples. The degradation pattern of α-2-M in serum or plasma corresponded to the pattern observed with purified α-2-M. Thus, the described immunoblotting technique, applied directly to serum or plasma, could detect all not heat-denaturated α-2-M products as seen on Coomassie-stained polyacrylamide gels when analyzing purified α-2-M." @default.
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• W1993627674 date "1985-01-01" @default.
• W1993627674 modified "2023-09-24" @default.
• W1993627674 title "Application of the immunoblotting technique to the study of single protein species in complex biological fluids: A model study with alpha-2-macroglobulin" @default.
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• W1993627674 doi "https://doi.org/10.1002/elps.1150060506" @default.
• W1993627674 hasPublicationYear "1985" @default.
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