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Resistance of structure and antigenic determinations of native hexon of type 1 adenovirus to protease

Journal Article · · Biochemistry (Engl. Transl.); (United States)
OSTI ID:5879218
Native hexon capsomers (trimers) of human type 1 adenovirus (Ad hl) were labeled with /sup 125/I and subjected to cleavage by trypsin, chymotrypsin, and papain. The hydrolysis of the hexon of Ad 1 by these enzymes is limited and in each case a set of relatively large fragments, which are not cleaved during prolonged hydrolysis, is formed. The degree of hydrolysis of the Ad hl hexon increases in the order trypsin < chymotrypsin < papain, the molecular weight of the largest fragments constituting 80,000, 40,000, and 32,000, respectively. At a decreased temperature all the large fragments of the hydrolysates obtained are confined in aggregates (the cores of the hexon), similar in structure to the original hexon trimers, the papain core of the Ad hl hexon being the most stable during electrophoresis in polyacrylamide gel and the chymotrypsin core being the least. A radioimmunoprecipitation analysis showed that denatured fragments of the tryptic, chymotryptic, and papain hydrolysates do not possess antigenic activity.
Research Organization:
D.K. Zabolotnii Institute of Microbiology and Virology, Kiev, USSR
OSTI ID:
5879218
Journal Information:
Biochemistry (Engl. Transl.); (United States), Journal Name: Biochemistry (Engl. Transl.); (United States) Vol. 51:8; ISSN BIORA
Country of Publication:
United States
Language:
English