Expression of goat α-lactalbumin in Escherichia coli and its refolding to biologically active protein

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Abstract
Expression of functionally active bovine visual rhodopsin was achieved by sequential transcription and translation in vitro of rhodopsin gene cDNA with co-translational insertion of the protein into phosphatidylcholine liposomes. The recombinant rhodopsin has functional, spectral and immunochemical properties similar to those of natural rhodopsin from bovine retina. Two mutant rhodopsins, Cys316 – Ser and Asp330 – Asn, Asp331 – Asn, were produced by oligonucleotidedirected mutagenesis. The first mutation does not affect rhodopsin's ability to stimulate transducin GTPase and visual cGMP phosphodiesterase activities, while the second double mutation leads to a sharp decrease in rhodopsin activity.