Structure and organ specificity of an anionic peroxidase from Arabidopsis thaliana cell suspension culture

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Standard

Structure and organ specificity of an anionic peroxidase from Arabidopsis thaliana cell suspension culture. / Ostergaard, L; Abelskov, A K; Mattsson, O; Welinder, K G.

I: FEBS Letters, Bind 398, Nr. 2-3, 1996, s. 243-7.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Ostergaard, L, Abelskov, AK, Mattsson, O & Welinder, KG 1996, 'Structure and organ specificity of an anionic peroxidase from Arabidopsis thaliana cell suspension culture', FEBS Letters, bind 398, nr. 2-3, s. 243-7.

APA

Ostergaard, L., Abelskov, A. K., Mattsson, O., & Welinder, K. G. (1996). Structure and organ specificity of an anionic peroxidase from Arabidopsis thaliana cell suspension culture. FEBS Letters, 398(2-3), 243-7.

Vancouver

Ostergaard L, Abelskov AK, Mattsson O, Welinder KG. Structure and organ specificity of an anionic peroxidase from Arabidopsis thaliana cell suspension culture. FEBS Letters. 1996;398(2-3):243-7.

Author

Ostergaard, L ; Abelskov, A K ; Mattsson, O ; Welinder, K G. / Structure and organ specificity of an anionic peroxidase from Arabidopsis thaliana cell suspension culture. I: FEBS Letters. 1996 ; Bind 398, Nr. 2-3. s. 243-7.

Bibtex

@article{dfc9cff0e62011ddbf70000ea68e967b,
title = "Structure and organ specificity of an anionic peroxidase from Arabidopsis thaliana cell suspension culture",
abstract = "The predominant peroxidase (pI 3.5) (E.C. 1.11.1.7) of an Arabidopsis thaliana cell suspension culture was purified and partially sequenced. Oligonucleotides were designed and a specific probe was obtained. A cDNA clone was isolated from an Arabidopsis cell suspension cDNA library and completely sequenced. The cDNA clone comprised 1194 bp and encodes a 30 residue signal peptide and a 305 residue mature protein (Mr 31,966). The sequence of the mature protein is 95% identical to the well-characterized horseradish peroxidase HRP A2 and has therefore been designated ATP A2. Three introns at positions identical to those found in Arabidopsis and horseradish genes encoding cationic peroxidases were identified. RT-PCR analysis revealed root-specific expression.",
author = "L Ostergaard and Abelskov, {A K} and O Mattsson and Welinder, {K G}",
note = "Keywords: Amino Acid Sequence; Arabidopsis; Base Sequence; Cloning, Molecular; DNA, Complementary; Gene Expression Regulation, Plant; Genes, Plant; Glycosylation; Introns; Isoelectric Point; Molecular Sequence Data; Peroxidase; Plant Roots; RNA, Messenger; RNA, Plant; Sequence Alignment",
year = "1996",
language = "English",
volume = "398",
pages = "243--7",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "2-3",

}

RIS

TY - JOUR

T1 - Structure and organ specificity of an anionic peroxidase from Arabidopsis thaliana cell suspension culture

AU - Ostergaard, L

AU - Abelskov, A K

AU - Mattsson, O

AU - Welinder, K G

N1 - Keywords: Amino Acid Sequence; Arabidopsis; Base Sequence; Cloning, Molecular; DNA, Complementary; Gene Expression Regulation, Plant; Genes, Plant; Glycosylation; Introns; Isoelectric Point; Molecular Sequence Data; Peroxidase; Plant Roots; RNA, Messenger; RNA, Plant; Sequence Alignment

PY - 1996

Y1 - 1996

N2 - The predominant peroxidase (pI 3.5) (E.C. 1.11.1.7) of an Arabidopsis thaliana cell suspension culture was purified and partially sequenced. Oligonucleotides were designed and a specific probe was obtained. A cDNA clone was isolated from an Arabidopsis cell suspension cDNA library and completely sequenced. The cDNA clone comprised 1194 bp and encodes a 30 residue signal peptide and a 305 residue mature protein (Mr 31,966). The sequence of the mature protein is 95% identical to the well-characterized horseradish peroxidase HRP A2 and has therefore been designated ATP A2. Three introns at positions identical to those found in Arabidopsis and horseradish genes encoding cationic peroxidases were identified. RT-PCR analysis revealed root-specific expression.

AB - The predominant peroxidase (pI 3.5) (E.C. 1.11.1.7) of an Arabidopsis thaliana cell suspension culture was purified and partially sequenced. Oligonucleotides were designed and a specific probe was obtained. A cDNA clone was isolated from an Arabidopsis cell suspension cDNA library and completely sequenced. The cDNA clone comprised 1194 bp and encodes a 30 residue signal peptide and a 305 residue mature protein (Mr 31,966). The sequence of the mature protein is 95% identical to the well-characterized horseradish peroxidase HRP A2 and has therefore been designated ATP A2. Three introns at positions identical to those found in Arabidopsis and horseradish genes encoding cationic peroxidases were identified. RT-PCR analysis revealed root-specific expression.

M3 - Journal article

C2 - 8977116

VL - 398

SP - 243

EP - 247

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 2-3

ER -

ID: 9831748