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

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

doi:10.1016/0014-5793(85)80238-6

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

J. Hejgaard^*, S. K. Rasmussen, A. Brandt, I. Svendsen

^*Corresponding author for this work

70 Citations (Scopus)

Abstract

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.

Original language	English
Journal	FEBS Letters
Volume	180
Issue number	1
Pages (from-to)	89-94
Number of pages	6
ISSN	0014-5793
DOIs	https://doi.org/10.1016/0014-5793(85)80238-6
Publication status	Published - 21 Jan 1985

Keywords

Amino acid sequence
Barley seed
Nucleotide sequence
Ovalbumin
Polyadenylation signal
Serine proteinase inhibitor

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10.1016/0014-5793(85)80238-6

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

abstract = "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.",

keywords = "Amino acid sequence, Barley seed, Nucleotide sequence, Ovalbumin, Polyadenylation signal, Serine proteinase inhibitor",

author = "J. Hejgaard and Rasmussen, {S. K.} and A. Brandt and I. Svendsen",

year = "1985",

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T1 - Sequence homology between barley endosperm protein Z and protease inhibitors of the α1-antitrypsin family

AU - Hejgaard, J.

AU - Rasmussen, S. K.

AU - Brandt, A.

AU - Svendsen, I.

PY - 1985/1/21

Y1 - 1985/1/21

N2 - 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.

AB - 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.

KW - Amino acid sequence

KW - Barley seed

KW - Nucleotide sequence

KW - Ovalbumin

KW - Polyadenylation signal

KW - Serine proteinase inhibitor

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DO - 10.1016/0014-5793(85)80238-6

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SN - 0014-5793

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SP - 89

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JO - F E B S Letters

JF - F E B S Letters

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

Abstract

Keywords

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