Sequence homology between barley endosperm protein Z and protease inhibitors of the α1-antitrypsin family
Research output: Contribution to journal › Journal article › Research › peer-review
Six cDNA clones encoding parts of protein Z, a major barley endosperm albumin, have been identified. Nucleotide and amino acid sequencing have established a 180 residues long C-terminal amino acid sequence of protein Z as well as two minor amino acid sequences (14 and 7 residues). These sequences show that barley protein Z is homologous with human α1-antitrypsin, human otj-antichymotrypsin, human antithrombin III, mouse contrapsin and chicken ovalbumin (26-32% of the 180 residues in the C-terminal sequence in identical positions). The sequence homology and specific cleavage of protein Z at a bond corresponding to the reactive site of the inhibitors indicate a possible inhibitory function. Inhibition of microbial or pancreatic serine proteases could, however, not be associated with protein Z.
|Number of pages||6|
|Publication status||Published - 21 Jan 1985|
- Amino acid sequence, Barley seed, Nucleotide sequence, Ovalbumin, Polyadenylation signal, Serine proteinase inhibitor