Complete amino acid sequence of the protease inhibitor BWI-4a from buckwheat seeds.
The complete amino acid sequence of the protease inhibitor BWI-4a from buckwheat (Fagopyrum esculentum Moench) seeds has been established by automated Edman degradation in combination with MALDI-TOF mass spectrometry. The inhibitor molecule consists of 67 amino acid residues with a single disulfide bond. Its N-terminus is blocked by a pyroglutamic acid residue. The reactive site of the inhibitor contains an Arg43-Asp44 bond. Mass spectrometry revealed that inhibitor BWI-4a is present in buckwheat seeds in two isoforms differing by a single amino acid substitution of Gly40 for Ala40. Analysis of the amino acid sequence of the BWI-4a inhibitor indicates that this inhibitor is a member of the potato proteinase inhibitor I family.
Belozersky
M A
MA
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119899, Russia. mbeloz@genebee.msu.su
Dunaevsky
Y E
YE
Musolyamov
A K
AK
Egorov
T A
TA
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D019612:Fagopyrum / Q000737:chemistry* / Q000235:genetics*; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification; D011480:Protease Inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid; D011198:Solanum tuberosum / Q000737:chemistry / Q000235:genetics
D010940:Plant Proteins; D011480:Protease Inhibitors; D020033:Protein Isoforms