Complete amino acid sequence of mung bean trypsin inhibitor.

The mung bean trypsin inhibitor has been found to be microheterogeneous at N-terminal region due to the presence of several isomers. After treatment with aminopeptidase M it becomes homogeneous and is suitable for sequence determination. Based on the determination of the structures of two active fragments the complete amino acid sequence of mung bean trypsin inhibitor has been elucidated. It consists of 72 amino acid residues with 7 pairs of disulfide bonds. The results show that this inhibitor belongs to the Bowman-Birk inhibitor family.