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Processing of Fusion Proteins with Immobilized Factor Xa
Author(s) -
Assouline Zahra,
Graham Roger,
Miller Robert C.,
Warren R. Antony J.,
Kilburn Douglas G.
Publication year - 1995
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp00031a006
Subject(s) - agarose , chemistry , cellulose , fusion protein , combinatorial chemistry , chromatography , fusion , derivative (finance) , biochemistry , recombinant dna , linguistics , philosophy , financial economics , economics , gene
Factor Xa, with a cellulose‐binding domain (CBD) fused to the C‐terminus of the heavy chain (FXa‐CBD), is active in solution and when immobilized on cellulose. A second derivative of factor Xa in which a hexahistidine tail is fused to the C‐terminus of the heavy chain (FXa‐H 6 ) also retains activity when immobilized, in this case on Ni 2+ ‐NTA agarose. The stabilities and activities of FXa‐CBD and FXa‐H 6 immobilized on cellulose and Ni 2+ ‐NTA agarose, respectively, are similar. Immobilized factor Xa derivatives can be used to remove affinity tags from appropriate fusion proteins without contaminating the desired product with factor Xa.