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- W1969672009 abstract "Membrane proteins of intact erythrocytes were cross-linked using the cleavable homobifunctional reagent, 3,3'-dithiobis(propionimidate) and the non-cleavable heterobifunctional reagent, 4-azidobenzimidate. Subsequently, the exposed cross-linked membrane proteins were radiolabelled by the lactoperoxidase method. Cross-linked and radiolabelled membrane proteins were analyzed by two-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis in which resolution in the second dimension was preceded by mercaptoethanol treatment. Complexes so formed by 3,3'-dithiobis(propionimidate) were cleavable, whilst components cross-linked by 4-azidobenzimidate were uncleavable. Three complexes were found. Two of these contained protein III as the only radiolabelled component. It was assumed that the first (Mr approx. 200000) represents a dimer and the second (Mr approx. 300000) an oligomer of protein III. The third complex, which was identified after cross-linking with 4-azidobenzimidate, consisted of PAS II and a low molecular weight (lipid-like) component. Since PAS I (dimer of a PAS II) was not associated with this component it was concluded that PAS I and PAS II are situated in different environments of the erythrocyte membrane." @default.
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- W1969672009 date "1980-01-01" @default.
- W1969672009 modified "2023-09-26" @default.
- W1969672009 title "The Detection of Associated Erythrocyte Membrane Proteins by Cross-Linking and Surface Radiolabelling" @default.
- W1969672009 doi "https://doi.org/10.1515/bchm2.1980.361.1.885" @default.
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