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The complete amino acid sequence of the α‐amylase inhibitor I‐2 from seeds of ragi (Indian finger millet, Eleusine coracana Gaertn.)
Author(s) -
Campos F.A.P.,
Richardson M.
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)80130-1
Subject(s) - eleusine , thermolysin , chymotrypsin , biochemistry , amylase , trypsin , methionine , trypsin inhibitor , amino acid , tryptophan , peptide sequence , kunitz sti protease inhibitor , chemistry , alanine , biology , enzyme , finger millet , gene , agronomy
The complete amino acid sequence of the α‐amylase inhibitor I‐2 from ragi seeds was determined by analysis of peptides derived from the protein by digestion with trypsin, chymotrypsin thermolysin and S. aureus V8 protease. The protein consists of a single polypeptide chain of 95 amino acids, with a high content of serine and alanine, and no methionine, phenylalanine, histidine or tryptophan. There is no sequence homology with the bifunctional α‐amylase/trypsin inhibitor in the same seeds or with any of the α‐amylase inhibitors from other plants. The sequence contains two regions of weakly repetitive internal homology. The predicted secondary structure of the inhibitor is notable for the absence of α‐helix and its high content (50%) of β‐turn.