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- W2378718150 abstract "Objective To obtain high yield of recombinant human apolipoprotein A-Ⅰ(apoA-Ⅰ) with normal structural and functional properties by a prokaryotic expression system.Methods PET-30b(+) was used as an expression vector,silent mutation was introduced to increase the expression yield,and a 6×histine tag was added to the C-terminus to facilitate purification.α helical content,capabilities of binding lipid and promoting cellular cholesterol efflux were examined for recombinant protein.Results A high yield up to(12 mg) purified apoA-Ⅰ per(1 L) bacterial culture was obtained.To the recombinant apoA-Ⅰ,α helical content,rate constant(k_(1/2)) of lipid binding kinetics and fraction of cholesterol efflux were(54±4)%,(0.059±(0.002)min~(-1)),and(16.68±1.77)% respectively.(Conclusion This) expression system is very useful to generate apoA-Ⅰ or its mutants." @default.
- W2378718150 created "2016-06-24" @default.
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- W2378718150 date "2006-01-01" @default.
- W2378718150 modified "2023-09-24" @default.
- W2378718150 title "Prokaryotic expression of human apolipoprotein A-I and characterizations of secondary structure and functions" @default.
- W2378718150 hasPublicationYear "2006" @default.
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