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Characterization of a bifunctional wheat inhibitor of endogenous α‐amylase and subtilisin
Author(s) -
Mundy J.,
Hejgaard J.,
Svendsen I.
Publication year - 1984
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(84)80128-3
Subject(s) - subtilisin , serine protease , bifunctional , biochemistry , amylase , trypsin inhibitor , kunitz sti protease inhibitor , chemistry , protease inhibitor (pharmacology) , trypsin , protease , chymotrypsin , enzyme , biology , genetics , virus , antiretroviral therapy , viral load , catalysis
A bifunctional α‐amylase/serine protease inhibitor which inhibits germination‐specific cereal α‐amylases of the Graminae subfamily Festucoideae as well as bacterial subtilisins has been isolated from wheat grains. This protein has M r ≈20500 and p I ≈7.2. The amino acid composition and N‐teminal sequence (45 residues) show that the inhibitor is homologous with cereal and leguminous inhibitors of the soybean trypsin inhibitor (Kunitz) family.