Retinol binding protein IV purified from Escherichia coli using intein-mediated cleavage as a suitable replacement for serum sources.

Est, Chandler B; Murphy, Regina M

Est, Chandler B; Murphy, Regina M.

Affiliation

Est CB; Department of Chemical and Biological Engineering, University of Wisconsin - Madison, 1415 Engineering Dr., Madison, WI, 53706, USA.
Murphy RM; Department of Chemical and Biological Engineering, University of Wisconsin - Madison, 1415 Engineering Dr., Madison, WI, 53706, USA. Electronic address: regina.murphy@wisc.edu.

Protein Expr Purif ; 167: 105542, 2020 03.

Article in En | MEDLINE | ID: mdl-31756375

Subject(s)

Recombinant Proteins/isolation & purification; Retinol-Binding Proteins/biosynthesis; Retinol-Binding Proteins/isolation & purification; Escherichia coli/genetics; Escherichia coli/metabolism; Genes, Bacterial; Humans; Inteins/genetics; Recombinant Proteins/biosynthesis; Recombinant Proteins/chemistry; Retinol-Binding Proteins/chemistry; Vitamin A/blood; Vitamin A/chemistry

Key words

Inteins; Oxidative refolding; Retinol; Retinol binding protein; Transthyretin

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Recombinant Proteins / Retinol-Binding Proteins Limits: Humans Language: En Journal: Protein Expr Purif Journal subject: BIOLOGIA MOLECULAR Year: 2020 Type: Article Affiliation country: United States

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