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

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Sequence homology between barley endosperm protein Z and protease inhibitors of the α1-antitrypsin family. / Hejgaard, J.; Rasmussen, S. K.; Brandt, A.; Svendsen, I.

In: FEBS Letters, Vol. 180, No. 1, 21.01.1985, p. 89-94.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Hejgaard, J, Rasmussen, SK, Brandt, A & Svendsen, I 1985, 'Sequence homology between barley endosperm protein Z and protease inhibitors of the α1-antitrypsin family', FEBS Letters, vol. 180, no. 1, pp. 89-94. https://doi.org/10.1016/0014-5793(85)80238-6

APA

Hejgaard, J., Rasmussen, S. K., Brandt, A., & Svendsen, I. (1985). Sequence homology between barley endosperm protein Z and protease inhibitors of the α1-antitrypsin family. FEBS Letters, 180(1), 89-94. https://doi.org/10.1016/0014-5793(85)80238-6

Vancouver

Hejgaard J, Rasmussen SK, Brandt A, Svendsen I. Sequence homology between barley endosperm protein Z and protease inhibitors of the α1-antitrypsin family. FEBS Letters. 1985 Jan 21;180(1):89-94. https://doi.org/10.1016/0014-5793(85)80238-6

Author

Hejgaard, J. ; Rasmussen, S. K. ; Brandt, A. ; Svendsen, I. / Sequence homology between barley endosperm protein Z and protease inhibitors of the α1-antitrypsin family. In: FEBS Letters. 1985 ; Vol. 180, No. 1. pp. 89-94.

Bibtex

@article{c1084e632672451b9d362c050b90cd9d,
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,
day = "21",
doi = "10.1016/0014-5793(85)80238-6",
language = "English",
volume = "180",
pages = "89--94",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "1",

}

RIS

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

UR - http://www.scopus.com/inward/record.url?scp=0001813953&partnerID=8YFLogxK

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

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

M3 - Journal article

AN - SCOPUS:0001813953

VL - 180

SP - 89

EP - 94

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 1

ER -

ID: 204471987