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Updated: May 23, 2026

Rapid High-throughput Species Identification of Botanical Material Using Direct Analysis in Real Time High Resolution Mass Spectrometry
Published on: October 2, 2016
Activity based insights into the seed proteins of Datura alba from Pakistan
Tehreem Abdul Hameed1, Laraib Batool1, Ifrah Siddiqui2
1Dr. Zafar H Zaidi Center for Proteomics, University of Karachi, Karachi, Pakistan.
Background:
There are fifteen species of Datura, a perennial shrub-like herb, with Datura alba (D. alba) being the most important medicinal plant because of its therapeutic and aesthetic uses. Pharmaceutical goods use fresh seeds, fresh leaves, roots, dried leaves, dried mature seeds and fruits of D. alba. Seed proteins are the plant component most often overlooked for use in complementary and alternative medicine, even though all plant parts have nearly identical therapeutic properties and effects. This results from a deficiency of knowledge on the components of proteins.
Objectives:
The current study is to extract proteins from D. alba plant seeds in order to show data that will identify few major enzymes in the whole protein extract.
Methods:
The protein chemistry techniques, such as gel electrophoresis and chromatography, have been applied for seed protein analysis. After extraction of seed proteins in PBS (pH 7.4) buffer, the chromatography using DEAE Sephacryl (macroprep) resin, SDS-PAGE, zymography and biochemical tests were performed.
Results:
There were three distinct peaks identified by the chromatographic separation. Protein bands were visible in the reduced and non-reduced SDS-PAGE analysis, while the results of substrate zymography indicated the presence of proteases and phospholipases. Strong antioxidant activity and antibiofilm activity on MRSA were also observed in the D. alba seeds proteins.
Conclusion:
Enzymatic and biochemical activities were observed with the protein extract obtained from the seeds of D. alba. Fractions of the proteins were also active and showed separation of protein components on the basis of ionic strength.
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