Heterotetramer
A heterotetramer is protein containing four non-covalently bound subunits, wherein the subunits are not all identical.[1] A homotetramer contains four identical subunits.[2]
Examples include haemoglobin (pictured), the NMDA receptor, some aquaporins,[3] some AMPA receptors, as well as some enzymes.[4]
Purification of heterotetramers
Ion-exchange chromatography is useful for isolating specific heterotetrameric protein assemblies, allowing purification of specific complexes according to both the number and the position of charged peptide tags.[5][6] Nickel affinity chromatography may also be employed for heterotetramer purification.[7]
See also
References
- ↑ "GO term: protein heterotetramerization". YeastGenome. Retrieved 14 May 2011.
- ↑ "GO term: protein homotetramerization". YeastGenome. Retrieved 14 May 2011.
- ↑ Neely, John D.; Christensen, Birgitte M.; Nielsen, Søren; Agre, Peter (1 August 1999). "Heterotetrameric Composition of Aquaporin-4 Water Channels". Biochemistry 38 (34): 11156–63. doi:10.1021/bi990941s. PMID 10460172.
- ↑ Chang, T.-H.; Hsieh, F.-L.; Ko, T.-P.; Teng, K.-H.; Liang, P.-H.; Wang, A. H.-J. (5 February 2010). "Structure of a Heterotetrameric Geranyl Pyrophosphate Synthase from Mint (Mentha piperita) Reveals Intersubunit Regulation". Plant Cell 22 (2): 454–467. doi:10.1105/tpc.109.071738. PMC 2845413. PMID 20139160.
- ↑ Sakash, J.B.; Kantrowitz, E.R. (2000). "The contribution of individual interchain interactions to the stabilization of the T and R states of Escherichia coli aspartate transcarbamoylase.". J Biol Chem 275 (37): 28701–7. doi:10.1074/jbc.M005079200. PMID 10875936.
- ↑ Fairhead, M. (2013). "Plug-and-Play Pairing via Defined Divalent Streptavidins.". J Mol Biol 426 (1): 199–214. doi:10.1016/j.jmb.2013.09.016. PMID 24056174.
- ↑ Howarth, Mark; Chinnapen, Daniel J-F; Gerrow, Kimberly; Dorrestein, Pieter C; Grandy, Melanie R; Kelleher, Neil L; El-Husseini, Alaa; Ting, Alice Y (2006). "A monovalent streptavidin with a single femtomolar biotin binding site". Nature Methods 3 (4): 267–73. doi:10.1038/nmeth861. PMC 2576293. PMID 16554831.