Purification and characterization of RGA2, a Rho2 GTPase-activating protein from Tinospora cordifolia

By Mohd. Amir, Mohammad Aasif Dar, Wahiduzzaman, Asimul Islam, Faizan Ahmad, Imtaiyaz Hassan

August 13, 2018

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Title

Purification and characterization of RGA2, a Rho2 GTPase-activating protein from Tinospora cordifolia

Author

Mohd. Amir, Mohammad Aasif Dar, Wahiduzzaman, Asimul Islam, Faizan Ahmad, Imtaiyaz Hassan

Year

2016

Journal

3 Biotech

Abstract

Rho GTPases activating protein 2 (RGA2) is primarily involved in the modulation of numerous morphological events in eukaryotes. It protects plants by triggering the defense system which restricts the pathogen growth. This is the first report on the isolation, purification and characterization of RGA2 from the stems of Tinospora cordifolia, a medicinal plant. The RGA2 was purified using simple two-step process using DEAE-Hi-Trap FF and Superdex 200 chromatography columns, with a high yield. The purity of RGA2 was confirmed by SDS-PAGE and identified by MALDI-TOF/MS. The purified protein was further characterized for its secondary structural elements using the far-UV circular dichroism measurements. Our purification procedure is simple two-step process with high yield which can be further used to produce RGA2 for structural and functional studies.

Full Article

https://link.springer.com/article/10.1007/s13205-016-0400-3

Instrument

J-1500

Keywords

Circular dichroism, Secondary structure, Thermal stability, Biochemistry