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In experiments on isolated human erythrocyte membranes, cross-links between protein components have been produced both by the catalyzed oxidation of intrinsic sulfhydryl groups with the o-phenanthroline cupric ion complex and by reaction with dimethyl dithiobispropionimidate, a bisalkylimidate containing a disulfide linkage between the two reactive groups. The mixture of molecular species has been analyzed by a two-dimensional gel electrophoresis procedure in which the cross-links are split by reductive cleavage during an initial phase of the separation in the second dimension. Cross-linked complexes are recognized by the positions of the off-diagonal elements in the final pattern.

Complexes apparently derived from stable oligomers of peptides of the same molecular weight have been found corresponding to many of the bands in the standard sodium dodecyl sulfate gel pattern. Heterocomplexes formed …