In this section
@article{Singh:2012:10.1002/0471140864.ps2904s67,
author = {Singh, S and Zhang, M and Bertheleme, N and Strange, PG and Byrne, B},
doi = {10.1002/0471140864.ps2904s67},
journal = {Curr Protoc Protein Sci},
pages = {29.4.1--29.4.17},
title = {Purification of the human G protein-coupled receptor adenosine A(2a)R in a stable and functional form expressed in Pichia pastoris.},
url = {http://dx.doi.org/10.1002/0471140864.ps2904s67},
volume = {Chapter 29},
year = {2012}
}
TY - JOUR
AB - The isolation of membrane proteins with the aim of producing highly pure, homogeneous, stable, and functional material remains challenging, and it is often necessary to develop protein-specific purification protocols by trial and error. One key tool that is required in the development of a suitable protocol is a functional assay. This unit describes a range of different protocols for isolation of the human adenosine A2a receptor (A(2a)R). These protocols show the importance of developing a robust method for comparing the quality of protein obtained by a combination of biophysical analyses including SDS-PAGE, analytical size-exclusion chromatography, and functional analysis. One of the keys to isolating and maintaining a functional receptor, found not only in the optimal protocol described here but in other published examples, is that there should be no more than two chromatographic steps.
AU - Singh,S
AU - Zhang,M
AU - Bertheleme,N
AU - Strange,PG
AU - Byrne,B
DO - 10.1002/0471140864.ps2904s67
EP - 4
PY - 2012///
SP - 29
TI - Purification of the human G protein-coupled receptor adenosine A(2a)R in a stable and functional form expressed in Pichia pastoris.
T2 - Curr Protoc Protein Sci
UR - http://dx.doi.org/10.1002/0471140864.ps2904s67
UR - https://www.ncbi.nlm.nih.gov/pubmed/22294329
VL - Chapter 29
ER -
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