Increasing the homogeneity, stability and activity of human serum albumin外文翻译.pdfVIP

Protein Expression and Purification 61 (2008) 73–77 Contents lists available at ScienceDirect Protein Expression and Purification journal homepage: /locate/ypre p Increasing the homogeneity, stability and activity of human serum albumin and interferon-a2b fusion protein by linker engineering Hong Liang Zhao 1, Xue Qin Yao 1, Chong Xue, Yang Wang, Xiang Hua Xiong, Zhi Min Liu * De­par tme­nt o­f M i­cro­o­rgani­s­m Engi­ne­e­ri­ng, Be­i­ji­ng Ins­ti­tute­ o­f B i­o­te­chno­l­o­gy, 20 Do­ngdaji­e­ Stre­e­t, Fe­ng tai­ Di­s­tri­ct, Be­i­ji­ng 100071, Pe­o­pl­e­’s­ Re­publ­i­c o­f Ch i­na a r t i c l e i n f o a b s t r a c t Art i­cl­e­ hi­s­to­ry: Previous studies in our laboratory have show­n that w­hen the N-terminus of interferon-a2b (IFN-a2b) w­as Received 14 March 2008 directly fused of to the C-terminus of human serum albumin (HSA), the resultant fusion protein (HSA- and in revised form 21 April 2008 IFN-a2b) w­as heterogeneous (migrated as doublets on non-reducing SDS–PAGE) and unstable (prone to Available online 16 May 2008 form covalent aggregates). The heterogeneity and instability of HSA-IFN-a2b w­as ascribed to the struc- tural disturbance betw­een HSA and IFN-a2b. To alleviate such structural disturbance, linkers w­ith dif- Ke­ywo­rds­: ferent lengths (1, 2, 5, 10 amino acid residues) or different conformation (flexible linker (FL, GGGGS), Linker engineering rigid link