Chemical Studies on Vesicant-treated Proteins

UTHSC Affiliation

College of Medicine

Document Type

Article

Publication Date

1-1-1942

Publication Title

Journal of Infectious Diseases

Volume

70

Issue

3

Abstract

A study was made of the cleavage by alkali of the linkages between protein and vesicant residues in preparations obtained by the treatment of insulin, pepsin and tobacco mosaic virus with benzyl ß-chloroethyl sulfide (benzyl-H) or n-butyl ß- chloroethyl sulfide (butyl-H) containing radiosulfur. The extent of liberation of vesicant residues varied with the different proteins; in all cases, a certain fraction of the vesicant residues was not cleaved by the alkali under the conditions studied. A more detailed investigation of the action of alkali on vesicant-treated insulin showed that the rate of liberation of vesicant residues was dependent upon the temperature and pH of treatment. Heating of vesicant-treated insulin at 150° in neutral solution also resulted in the liberation of vesicant residues. By application of the “washing-out” technique to the radiosulfur-containing material cleaved from butyl-H- or benzyl-H-treated insulin, the cleavage product was demonstrated to consist mainly of the corresponding alkyl ß-hydroxyethyl sulfide. Studies on vesicant-treated tobacco mosaic virus indicated that vesicant residues were attached to both the nucleic acid and protein moieties of the virus. © 1948, American Chemical Society. All rights reserved.

Share

COinS