Barley peroxidase isozymes: Expression and post-translational modification in mature seeds as identified by two-dimensional gel electrophoresis and mass spectrometry

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Standard

Barley peroxidase isozymes : Expression and post-translational modification in mature seeds as identified by two-dimensional gel electrophoresis and mass spectrometry. / Laugesen, Sabrina; Bak-Jensen, Kristian Sass; Hägglund, Per; Henriksen, Anette; Finnie, Christine; Svensson, Birte; Roepstorff, Peter.

In: International Journal of Mass Spectrometry, Vol. 268, No. 2-3, 2007, p. 244-253.

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

Harvard

Laugesen, S, Bak-Jensen, KS, Hägglund, P, Henriksen, A, Finnie, C, Svensson, B & Roepstorff, P 2007, 'Barley peroxidase isozymes: Expression and post-translational modification in mature seeds as identified by two-dimensional gel electrophoresis and mass spectrometry', International Journal of Mass Spectrometry, vol. 268, no. 2-3, pp. 244-253. https://doi.org/10.1016/j.ijms.2007.06.003

APA

Laugesen, S., Bak-Jensen, K. S., Hägglund, P., Henriksen, A., Finnie, C., Svensson, B., & Roepstorff, P. (2007). Barley peroxidase isozymes: Expression and post-translational modification in mature seeds as identified by two-dimensional gel electrophoresis and mass spectrometry. International Journal of Mass Spectrometry, 268(2-3), 244-253. https://doi.org/10.1016/j.ijms.2007.06.003

Vancouver

Laugesen S, Bak-Jensen KS, Hägglund P, Henriksen A, Finnie C, Svensson B et al. Barley peroxidase isozymes: Expression and post-translational modification in mature seeds as identified by two-dimensional gel electrophoresis and mass spectrometry. International Journal of Mass Spectrometry. 2007;268(2-3):244-253. https://doi.org/10.1016/j.ijms.2007.06.003

Author

Laugesen, Sabrina ; Bak-Jensen, Kristian Sass ; Hägglund, Per ; Henriksen, Anette ; Finnie, Christine ; Svensson, Birte ; Roepstorff, Peter. / Barley peroxidase isozymes : Expression and post-translational modification in mature seeds as identified by two-dimensional gel electrophoresis and mass spectrometry. In: International Journal of Mass Spectrometry. 2007 ; Vol. 268, No. 2-3. pp. 244-253.

Bibtex

@article{4bd7a9a9b07f4bf48fcba1c681668a5d,
title = "Barley peroxidase isozymes: Expression and post-translational modification in mature seeds as identified by two-dimensional gel electrophoresis and mass spectrometry",
abstract = "Thirteen peroxidase spots on two-dimensional gels were identified by comprehensive proteome analysis of the barley seed. Mass spectrometry tracked multiple forms of three different peroxidase isozymes: barley seed peroxidase 1, barley seed-specific peroxidase BP1 and a not previously identified putative barley peroxidase. The presence of multiple spots for each of the isozymes reflected variations in post-translational glycosylation and protein truncation. Complete sequence coverage was achieved by using a series of proteases and chromatographic resins for sample preparation prior to mass spectrometric analysis. Distinct peroxidase spot patterns divided the 16 cultivars tested into two groups. The distribution of the three isozymes in different seed tissues (endosperm, embryo, and aleurone layer) suggested the peroxidases to play individual albeit partially overlapping roles during germination. In summary, a subset of three peroxidase isozymes was found to occur in the seed, whereas products of four other barley peroxidase genes were not detected. The present analysis documents the selective expression profiles and post-translational modifications of isozymes from a large plant gene family.",
keywords = "Barley, Glycosylation, Peroxidase, Tissue localization, Truncation",
author = "Sabrina Laugesen and Bak-Jensen, {Kristian Sass} and Per H{\"a}gglund and Anette Henriksen and Christine Finnie and Birte Svensson and Peter Roepstorff",
year = "2007",
doi = "10.1016/j.ijms.2007.06.003",
language = "English",
volume = "268",
pages = "244--253",
journal = "International Journal of Mass Spectrometry",
issn = "1387-3806",
publisher = "Elsevier",
number = "2-3",

}

RIS

TY - JOUR

T1 - Barley peroxidase isozymes

T2 - Expression and post-translational modification in mature seeds as identified by two-dimensional gel electrophoresis and mass spectrometry

AU - Laugesen, Sabrina

AU - Bak-Jensen, Kristian Sass

AU - Hägglund, Per

AU - Henriksen, Anette

AU - Finnie, Christine

AU - Svensson, Birte

AU - Roepstorff, Peter

PY - 2007

Y1 - 2007

N2 - Thirteen peroxidase spots on two-dimensional gels were identified by comprehensive proteome analysis of the barley seed. Mass spectrometry tracked multiple forms of three different peroxidase isozymes: barley seed peroxidase 1, barley seed-specific peroxidase BP1 and a not previously identified putative barley peroxidase. The presence of multiple spots for each of the isozymes reflected variations in post-translational glycosylation and protein truncation. Complete sequence coverage was achieved by using a series of proteases and chromatographic resins for sample preparation prior to mass spectrometric analysis. Distinct peroxidase spot patterns divided the 16 cultivars tested into two groups. The distribution of the three isozymes in different seed tissues (endosperm, embryo, and aleurone layer) suggested the peroxidases to play individual albeit partially overlapping roles during germination. In summary, a subset of three peroxidase isozymes was found to occur in the seed, whereas products of four other barley peroxidase genes were not detected. The present analysis documents the selective expression profiles and post-translational modifications of isozymes from a large plant gene family.

AB - Thirteen peroxidase spots on two-dimensional gels were identified by comprehensive proteome analysis of the barley seed. Mass spectrometry tracked multiple forms of three different peroxidase isozymes: barley seed peroxidase 1, barley seed-specific peroxidase BP1 and a not previously identified putative barley peroxidase. The presence of multiple spots for each of the isozymes reflected variations in post-translational glycosylation and protein truncation. Complete sequence coverage was achieved by using a series of proteases and chromatographic resins for sample preparation prior to mass spectrometric analysis. Distinct peroxidase spot patterns divided the 16 cultivars tested into two groups. The distribution of the three isozymes in different seed tissues (endosperm, embryo, and aleurone layer) suggested the peroxidases to play individual albeit partially overlapping roles during germination. In summary, a subset of three peroxidase isozymes was found to occur in the seed, whereas products of four other barley peroxidase genes were not detected. The present analysis documents the selective expression profiles and post-translational modifications of isozymes from a large plant gene family.

KW - Barley

KW - Glycosylation

KW - Peroxidase

KW - Tissue localization

KW - Truncation

U2 - 10.1016/j.ijms.2007.06.003

DO - 10.1016/j.ijms.2007.06.003

M3 - Journal article

AN - SCOPUS:35748942555

VL - 268

SP - 244

EP - 253

JO - International Journal of Mass Spectrometry

JF - International Journal of Mass Spectrometry

SN - 1387-3806

IS - 2-3

ER -

ID: 240161048