Heterotetramer
From Infogalactic: the planetary knowledge core
The heterotetrameric molecule haemoglobin, made up of four subunits of two different types (coloured red and blue.)
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
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