Literature summary for 1.13.12.24 extracted from

Glynou, K.; Ioannou, P.C.; Christopoulos, T.K.
One-step purification and refolding of recombinant photoprotein aequorin by immobilized metal-ion affinity chromatography (2003), Protein Expr. Purif., 27, 384-390 .

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Application

Application	Comment	Organism
synthesis	overexpression of apoaequorin in Escherichia coli, solubilization of inclusion bodies with urea, purification and refolding of His6-apoaequorin in a single chromatographic step by immobilized metal-ion affinity chromatography using Ni2+-nitrilotriacetic acid agarose.The purity is greater than 80%, the yield is 0.71mg apoaequorin from a 50 ml bacterial culture. The luminescence of the purified aequorin is a linear function of its concentration extending over six orders of magnitude	Aequorea victoria

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Aequorea victoria

Organism

Organism	UniProt	Comment	Textmining
Aequorea victoria	P02592	-	-

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Release 2023.1 (January 2023)