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Proteome responses to herbicidal stress in maize

100%

Tyczewska A., Bielinska I., Gracz J., Sikora M., Twardowski T.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2015

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tom 96

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nr 1

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Primary results of 2-dimensional electrophoresis for protein studies of Gentiana kurroo Royle somatic embryos derived from long-term embryogenic cell suspensions

100%

Niedziela A., Rybczynski J. J.

Acta Societatis Botanicorum Poloniae

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2014

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tom 83

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nr 3

Two-dimensional gel electrophoresis was used to compare protein expression profiles between various stages of Gentiana kurroo Royle somatic embryos. Seven distinct stages (I–VII) were pointed out and measured from long-term embryogenic cell suspension. Isoelectric focusing was done in the pH intervals 3–10, and the second dimension was carried out with 13% SDS-polyacrylamide gel electrophoresis. Dependent on the stage from about 400 (stage IV) to more than 700 (stage II) protein spots were totally detected. The molecular weight of abundant proteins range from 12 to 70 kDa, however, majority of proteins were located between 20–49 kDa spots on the gels. The highest difference in the number of spots appeared in the case of globular embryo (stage I) and elongated cotyledonary stage (stage VII) with differences being about 130 spots. The relevance of embryogenic cell suspension choice for proteomic analysis as well as expediency of the increasing number of particular embryo stages is discussed.

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Preliminary analysis of the cauliflower mitochondrial proteome

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Pawlowski T., Rurek M., Janicka S., Raczynska K. D., Augustyniak H.

Acta Physiologiae Plantarum

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2005

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tom 27

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nr 3A

Purified cauliflower (Brassica oleracea var. botrytis) mitochondrial proteins fractionated into soluble, membrane, integral membrane and peripheral membrane samples were analyzed by 2D- PAGE (isoelectric focusing/ SDS polyacrylamide gel electrophoresis). 2D gels patterns were compared using the Imager Master 2D Elite software. 561 silver stained protein spots were resolved after electrophoresis under standard conditions of a whole protein extract. In the soluble fraction a prevalent number of more intense protein spots was observed. The cauliflower protein 2D patterns resembled Arabidopsis thaliana 2D patterns. The two protein spots selected which occupied a similar isoelectric point positions on both gels represented the same proteins as revealed by ESI-MS analysis of cauliflower proteins. The third selected spot belongs to unidentified proteins. The comparative analysis of mitochondrial suborganellar fractions proved the usefulness of this approach.

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Secretomic analysis of large cell lung cancer cell lines using two-dimensional gel electrophoresis coupled to mass spectrometry

84%

Yousefi Z., Sarvari J., Nakamura K., Kuramitsu Y., Ghaderi A., Mojtahedi Z.

Folia Histochemica et Cytobiologica

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2012

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tom 50

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nr 3

Ograniczanie wyników

1 Acta Physiologiae Plantarum

1 Acta Societatis Botanicorum Poloniae

1 BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

1 Folia Histochemica et Cytobiologica

1 Augustyniak H.

1 Bielinska I.

1 Ghaderi A.

1 Gracz J.

1 Janicka S.

1 Kuramitsu Y.

1 Mojtahedi Z.

1 Nakamura K.

1 Niedziela A.

1 Pawlowski T.

1 Raczynska K. D.

1 Rurek M.

1 Rybczynski J. J.

1 Sarvari J.

1 Sikora M.

1 Twardowski T.

1 Tyczewska A.

1 Yousefi Z.

1 2015

1 2014

1 2012

1 2005

Proteome responses to herbicidal stress in maize

Primary results of 2-dimensional electrophoresis for protein studies of Gentiana kurroo Royle somatic embryos derived from long-term embryogenic cell suspensions

Preliminary analysis of the cauliflower mitochondrial proteome

Secretomic analysis of large cell lung cancer cell lines using two-dimensional gel electrophoresis coupled to mass spectrometry