Sequence homology between barley trypsin inhibitor and wheat α‐amylase inhibitors

Structural relationship between barley (Hordeum vulgare) trypsin inhibitor and castor-bean (Ricinus communis) storage protein

“…Recently we have determined the complete amino acid sequence of barley (Hordeum vulgare) trypsin inhibitor (Odani et al, 1983), which was first isolated and characterized by Mikola & Suolina (1969). Formerly, we reported the unexpected sequence homology of this protein with wheat a-amylase inhibitor at tde N-terminal region (Odani et al, 1982), and this was confirmed by the complete sequence determination. Campos & Richardson (1983) also found that a bifunctional trypsin/a-amylase inhibitor from ragi (Eleusine coracana) is highly homologous with the barley and the wheat inhibitors.…”

New α-amylase and trypsin inhibitors among the CM-proteins of barley (Hordeum vulgare)

“…The determination of the N-terminal amino acid sequences of some of them has further supported this idea [7]. Furthermore, protein CMe has been found to be identical with a known trypsin inhibitor [5] and homologous to cereal a-amylase inhibitors [7,8]. Recently, weak homology has been found between these proteins and cereal storage proteins, such as y-secalins and a-gliadins [9].…”

Protease Inhibitors in Cereals

“…Another interesting point is that the barley eTI may be homologous with a wheat amylase inhibitor (Odani et al, 1982). If this suggestion is confirmed, the gene for the ancestor protein in wheat have probably been duplicated in an early wheat form and then evolved in two directions, one, resulting in a gene for the amylase inhibitor and one, resulting in a gene for the wheat eTI.…”