Determination of the primary structure of an alpha-amylase inhibitor from wheat kernel by Edman degradation and fast atom bombardment mass spectrometry.
The primary structure of an alpha-amylase inhibitor (coded 0.39) from wheat kernel was determined by fast atom bombardment mass spectrometry and Edman degradation. The sequence is similar to an extent of 97% compared to the other major component of the monomeric isoinhibitor family coded 0.28. The differences consist of the substitution of a single residue and the deletion of two residues in inhibitor 0.39. Neither heterogeneity nor polymorphism were observed in the primary structures of the inhibitors.
Caporale
C
C
Dipartimento di Agrobiologia ed Agrochimica, Università della Tuscia, Viterbo, Italy.
Carrano
L
L
Nitti
G
G
Poerio
E
E
Pucci
P
P
Buonocore
V
V
D000595:Amino Acid Sequence; D000681:Amylases / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000302:isolation & purification; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D010940:Plant Proteins; D016415:Sequence Alignment; D016339:Spectrometry, Mass, Fast Atom Bombardment; D014908:Triticum / Q000737:chemistry*; D014361:Trypsin Inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D000516:alpha-Amylases / Q000037:antagonists & inhibitors
D010446:Peptide Fragments; D010940:Plant Proteins; D014361:Trypsin Inhibitors; D000681:Amylases; D000516:alpha-Amylases