|The process of protein isolation and purification to conduct important procedures in a lab can be very difficult to perform. Usually, specialized chromatography resins are made by attaching a pure protein to the surface of the resin. This protein is then used as bait to bind to the protein that needs to be purified. These conventional processes generally require purification of the protein both before and after labeling, are non-selective either in amino acid site or side-chain chemistry for the protein, and can decrease the ability of the protein to bind and activate its target proteins. There is a critical need for a process to make affinity chromatography resins that can be used to purify proteins with minimal complications.
Researchers at Purdue University have found a novel method of making affinity chromatography resins for protein purification that is much simpler. By looking at the activity of calcium/calmodulin proteins, researchers found that specific proteins can be tagged with an azide tag and attached to an alkyne substrate immediately from the cell lysate mixture. The advantages of this process are that it simplifies the method by allowing conjugation in a direct manner and purifies a larger quantity of proteins. This would be useful in numerous research laboratories and experimental procedures given its efficiency.
-Protein specific tagging
-Direct manner of conjugation
-Purification of larger amount of proteins
Kulkarni, Chethana, et al. Bioorthogonal Chemoenzymatic Functionalization of Calmodulin for Bioconjugation Applications. Bioconjugate Chemistry. 2015, 26 (10), pp 2153–2160.
Feb 16, 2016
Feb 16, 2015
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