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The complete amino acid sequence of the bifunctional α‐amylase/trypsin inhibitor from seeds of ragi (Indian finger millet, Eleusine coracana Gaertn.)
Author(s) -
Campos F.A.P.,
Richardson M.
Publication year - 1983
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(83)80400-1
Subject(s) - eleusine , cyanogen bromide , trypsin , protease , biochemistry , chymotrypsin , thermolysin , amino acid , trypsin inhibitor , chemistry , amylase , kunitz sti protease inhibitor , peptide sequence , biology , enzyme , finger millet , agronomy , gene
The complete amino acid sequence of the bifunctional α‐amylase/trypsin inhibitor from ragi seeds was determined by analysis of fragments and peptides derived from the protein by cleavage with cyanogen bromide and by digestion with trypsin, chymotrypsin, thermolysin, the S. aureus V8 protease and a Pro‐specific protease. The molecular consists of a single polypeptide chain of 122 amino acids which exhibits sequence homology with trypsin inhibitors from barley and maize and with an α‐amylase inhibitor from wheat.