By Simon Roe
Makes a speciality of unit operations and analytical concepts and contains an summary of purification approach. Covers preliminary extraction and rationalization strategies, key purification tools with an emphasis on chromatography, and scale-up concerns. Hardcover, softcover additionally to be had.
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This fusion can be expressed in large amounts using a strong promoter and translation initiation signals of MBP. A one-step affinity purification for MBP is used to purify the fusion protein. The system contains pMAL vectors, which include convenient cloning sites for the gene of interest. Fusion protein yields of up to 100 mg from a litre of culture are claimed for this system. g. factor Xa. This sequence allows cleavage of the target protein after purification on the amylose resin affinity column.
Wood and A. R. Coker University of Southampton, School of Biological Sciences, Biomedical Sciences Building, Bassett Crescent East, Southampton S016 7PX, UK. 1 Introduction In the early days of protein biochemistry, crystallization was often employed as a purification technique and crystalliniry was considered an index of purity. Crystallographic studies were focused on a selection of proteins whose principle qualification was their abundance and ease of crystallization. The techniques of protein crystallography have now developed to such a degree that a complete three-dimensional structure analysis may not be a long task.
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