Reversibility of Denaturation of the Zymogen and the Proteolyzed Zymogen of Streptococcal Proteinase
Year: 1970
Type: article
Abstract: The single, uncross-linked polypeptide chain of the zymogen of the streptococcal proteinase is unfolded to a random structure in 6 m guanidinium chloride. When the denaturing agent is removed by dialysis, the potential enzymatic activity after tryptic hydrolysis and reduction is recoverable in 90% yield. Data on the unfolding process have been obtained by enzymatic assays and by optical rotatory dispersion. The zymogen also refolds after being heated at 100° for 10 min at pH 6.7 or after treatment with 0.1 n HCl for 2 hours at 25°. The proteolyzed zymogen, in which the first 100 residues from the NH2 terminus of the parent molecule have been removed, is irreversibly denatured under the same conditions. The NH2-terminal portion of the zymogen is thus necessary for the re-formation of the catalytically active molecule from the fully unfolded chain in this zymogen-enzyme system.
Source: Journal of Biological Chemistry
Authors: Michael C. Lin, Michael Bustin
Institution: Rockefeller University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1671510321