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Sequence homology between barley endosperm protein Z and protease inhibitors of the α1-antitrypsin family

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  • J. Hejgaard
  • S. K. Rasmussen
  • A. Brandt
  • I. Svendsen

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.

OriginalsprogEngelsk
TidsskriftFEBS letters
Vol/bind180
Udgave nummer1
Sider (fra-til)89-94
Antal sider6
ISSN0014-5793
DOI
StatusUdgivet - 21 jan. 1985

ID: 204471987