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 af dette arbejde

70 Citationer (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.

Originalsprog	Engelsk
Tidsskrift	FEBS Letters
Vol/bind	180
Udgave nummer	1
Sider (fra-til)	89-94
Antal sider	6
ISSN	0014-5793
DOI	https://doi.org/10.1016/0014-5793(85)80238-6
Status	Udgivet - 21 jan. 1985

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Citationsformater

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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",

month = jan,

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doi = "10.1016/0014-5793(85)80238-6",

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journal = "FEBS Letters",

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TY - JOUR

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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U2 - 10.1016/0014-5793(85)80238-6

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

M3 - Journal article

AN - SCOPUS:0001813953

SN - 0014-5793

VL - 180

SP - 89

EP - 94

JO - FEBS Letters

JF - FEBS Letters

IS - 1