Purification of correctly oxidized MHC class I heavy-chain molecules under denaturing conditions: A novel strategy exploiting disulfide assisted protein folding

Protein Science

Volumn 12, Issue 3, 2003, Pages 551-559

  Ferré, Henrik ^a,b   Ruffet, Emmanuel ^a   Blicher, Thomas ^a   Sylvester Hvid, Christina ^a   Nielsen, Lise Lotte B ^a   Hobley, Timothy J ^b   Thomas, Owen R T ^b   Buus, Søren ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b TECHNICAL UNIVERSITY OF DENMARK   (Denmark)

Author keywords

Disulfide bond formation; Hydrophobic interaction chromatography; Inclusion bodies; MHC class I; Protein folding

Indexed keywords

IMMUNOGLOBULIN HEAVY CHAIN; MACROGLOBULIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1;

ARTICLE; BINDING AFFINITY; BINDING KINETICS; CHROMATOGRAPHY; DENATURATION; DISULFIDE BOND; ENZYME LINKED IMMUNOSORBENT ASSAY; HYDROPHOBICITY; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN PURIFICATION;

ANIMALS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME-LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI; HISTOCOMPATIBILITY ANTIGENS CLASS I; HUMANS; IODINE RADIOISOTOPES; MICE; OXIDATION-REDUCTION; PEPTIDE FRAGMENTS; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; SUBCELLULAR FRACTIONS;

EID: 0037372546     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0233003     Document Type: Article

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