The selective chloromercuration of insulin.

A procedure has been described for the modification of the amino group of glycine methyl ester, and the amino groups of the hormone, insulin, with the reagent p-nitrophenyl-p-chloromercuribenzoate, effecting the introduction of the chloromercuri group at various defined sites in the protein molecule. Reaction for 30 min in dimethylformamide afforded several p-chloromercuribenzoyl-insulin derivatives which were characterized by DEAE-Sephadex and Sephadex G-50 chromatography, amino acid analysis, ultraviolet spectroscopy, deamination and trypsin digestion. These derivatives were also shown to possess high biological activity as judged by the glucose oxidation and radioimmunoassays.