Prokaryotic soluble overexpression and purification of bioactive human growth hormone by fusion to thioredoxin, maltose binding protein, and protein disulfide isomerase

PLoS ONE

Volumn 9, Issue 3, 2014, Pages

  Nguyen, Minh Tan ^a   Koo, Bon Kyung ^a   Thi Vu, Thu Trang ^a   Song, Jung A ^a   Chong, Seon Ha ^a   Jeong, Boram ^a   Ryu, Han Bong ^a   Moh, Sang Hyun ^b   Choe, Han ^a  

^a University of Ulsan College of Medicine   (South Korea)

^b BIO FD and C Co   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

GROWTH HORMONE DERIVATIVE; HUMAN GROWTH HORMONE; HUMAN GROWTH HORMONE HEXAHISTIDINE FUSION PROTEIN; HUMAN GROWTH HORMONE MALTOSE BINDING PROTEIN; HUMAN GROWTH HORMONE N UTILIZATION SUBSTANCE A FUSION PROTEIN; HUMAN GROWTH HORMONE PROTEIN DISULFIDE ISOMERASE; HUMAN GROWTH HORMONE THIOREDOXIN FUSION PROTEIN; HYBRID PROTEIN; UNCLASSIFIED DRUG; MALTOSE BINDING PROTEIN; PROTEIN DISULFIDE ISOMERASE; THIOREDOXIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CODON; CONTROLLED STUDY; DISULFIDE BOND; DRUG MECHANISM; DRUG PURIFICATION; DRUG SOLUBILITY; ESCHERICHIA COLI; GEL FILTRATION CHROMATOGRAPHY; GENE OVEREXPRESSION; MASS SPECTROMETRY; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN DOMAIN; TEMPERATURE SENSITIVITY; AMINO ACID SEQUENCE; ANIMAL; CELL FRACTIONATION; CELL LINE; CELL PROLIFERATION; CHEMISTRY; DRUG EFFECTS; HUMAN; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; PLASMID; PROKARYOTIC CELL; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; RAT; SOLUBILITY;

AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CELL PROLIFERATION; ESCHERICHIA COLI; HUMAN GROWTH HORMONE; HUMANS; MALTOSE-BINDING PROTEINS; MOLECULAR SEQUENCE DATA; PLASMIDS; PROKARYOTIC CELLS; PROTEIN DISULFIDE-ISOMERASES; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; RATS; RECOMBINANT FUSION PROTEINS; SOLUBILITY; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SUBCELLULAR FRACTIONS; THIOREDOXINS;

EID: 84897530802     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0089038     Document Type: Article

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