Complete amino acid sequence of the protease inhibitor from buckwheat seeds.
The complete amino acid sequence of protease inhibitor BWI-1 from buckwheat (Fagopyrum esculentum Moench) seeds has been established by automatic Edman degradation and mass spectrometry. The molecule of the inhibitor consists of 69 amino acid residues, with a molecular mass calculated as 7743.8 Da. The active site of the inhibitor contains an Arg45-Asp46 bond. Analysis of the amino acid sequence suggests that the buckwheat seed protease inhibitor is a member of the proteinase inhibitor I family.
Belozersky
M A
MA
A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russian Federation.
Dunaevsky
Y E
YE
Musolyamov
A X
AX
Egorov
T A
TA
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002523:Edible Grain / Q000737:chemistry*; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry*; D012639:Seeds / Q000737:chemistry; D014361:Trypsin Inhibitors / Q000737:chemistry*
D000596:Amino Acids; C095816:BWI-1 protein, Fagopyrum esculentum; D010940:Plant Proteins; D014361:Trypsin Inhibitors