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Journal Article

Protein profiling of non-model plant Cuminum cyminum by gel-based proteomic approach.

MPS-Authors
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Zaman,  U.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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2504297_Suppl.zip
(Supplementary material), 576KB

Citation

Zaman, U., Urlaub, H., & Abbasi, A. (2018). Protein profiling of non-model plant Cuminum cyminum by gel-based proteomic approach. Phytochemical Analysis, 29(3), 242-249. doi:10.1002/pca.2738.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002E-3793-2
Abstract
Introduction

Cumin (Cuminum cyminum), a popular spice has been widely used in traditional medicine to cure various ailments. Despite the existence of scientific literature about its pharmacological properties, no successful proteome profiling has yet been attempted.
Objective

To optimise extraction of cumin proteins and analyse its profile by shotgun proteomics, using one-dimensional electrophoresis coupled with nano-ESI-LC–MS/MS.
Methodology

As a first step, we have compared three extraction protocols for total proteins extraction from cumin. Extracted proteins were separated on one-dimensional gel and analysed by state-of-the-art linear ion trap (LTQ)-Orbitrap Velose and Q Exactive HF mass spectrometer.
Results

Evaluation of extraction method revealed significant differences in protein yield and proteome composition between the three extracts. LC–MS/MS allowed identification of several proteins with functional significance in various biological processes.
Conclusion

This study provides identification of a large number of proteins and offers a molecular basis for future research on potential pharmacologically active cumin proteins.