Abstract
The new compound 4-chloro-3,5-dinitrophenacyl bromide (CNPB) was studied as a potential polyfunctional protein reagent. Under mild experimental conditions the bromine atom, more reactive than the chlorine, is easily substituted by thiol groups. The amino groups in amino acids are not attacked, with the exception of phenylalanine, tyrosine and tryptophan, where a charge-transfer complex formed between the reagent and the aromatic nuclei of the amino acids facilitates the substitution of chlorine or bromine by the α-NH 2 groups. A reaction between the bromoacetyl moiety of the reagent and carboxylic acids is also possible. CNPB inactivates ribonuclease by substitution of approximately two histidyl residues accompanied by the formation of a π-complex, presumably with a vicinal aromatic residue.
Published Version
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