Premium
A new and general procedure for refolding mutant Bowman‐Birk‐type proteinase inhibitors on trypsin‐Sepharose as a matrix with complementary structure
Author(s) -
Flecker Peter
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80909-3
Subject(s) - trypsin , sepharose , chymotrypsin , serine , chemistry , biochemistry , amino acid , mutant , matrix (chemical analysis) , stoichiometry , enzyme , chromatography , organic chemistry , gene
The trypsin‐reactive subdomain of the Bowman‐Birk‐inhibitor of serine proteinases is shown to be highly vulnerable to perturbations induced by single amino acid replacements. Dramatic deviations from a stoichiometric 1:1 ratio to the chymotrypsin‐reactive subdomain used as an internal standard occur with all variants after renaturation in solution. A stoichiometric 1:1 ratio of subdomains is achieved via a new refolding procedure on trypsin‐Sepharose as a matrix with complementary structure.