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Sequence homology between barley endosperm protein Z and protease inhibitors of the α 1 ‐antitrypsin family
Author(s) -
Hejgaard J.,
Rasmussen S.K.,
Brandt A.,
Svendsen I.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80238-6
Subject(s) - biochemistry , peptide sequence , nucleic acid sequence , proteases , homology (biology) , biology , endosperm , complementary dna , protein primary structure , microbiology and biotechnology , amino acid , ovalbumin , protease , protein superfamily , chemistry , genetics , gene , enzyme , immune system
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 α 1 ‐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.