Uzma Zaman1,2,3, Henning Urlaub1,2, Atiya Abbasi4. 1. Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D-37077, Göttingen, Germany. 2. Bioanalytics Research Group, Department of Clinical Chemistry, University Medical Centre, Robert-Koch-Strasse 40, D-37075, Göttingen, Germany. 3. Dow Research Institute of Biotechnology and Biomedical Sciences, Dow University of Health Sciences, Gulzar-e-Hijri, Suparco Road, KDA Scheme -33, Karachi, Pakistan. 4. International Centre for Chemical and Biochemical Sciences (ICCBS), HEJ Research Institute of Chemistry, University of Karachi, Karachi, -75270, Pakistan.
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.
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.