The pro-sequence facilitates folding of human nerve growth factor from Escherichia coli inclusion bodies

European Journal of Biochemistry

Volumn 268, Issue 11, 2001, Pages 3296-3303

  Rattenholl, Anke ^a,b   Lilie, Hauke ^b   Grossmann, Adelbert ^c   Stern, Anne ^c   Schwarz, Elisabeth ^b   Rudolph, Rainer ^b  

^a UNIVERSITY OF MÜNSTER   (Germany)

^b MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

^c ROCHE DIAGNOSTICS GMBH   (Germany)

Author keywords

Cystine knot structural motif; Intramolecular chaperone; Nerve growth factor; Pro sequence; Renaturation

Indexed keywords

DIMER; NERVE GROWTH FACTOR BETA SUBUNIT; TRYPSIN;

AMINO ACID SEQUENCE; ARTICLE; CELL INCLUSION; CONTROLLED STUDY; DISULFIDE BOND; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN TRANSPORT; RENATURATION;

ELECTROPHORESIS, POLYACRYLAMIDE GEL; ELECTROPORATION; ESCHERICHIA COLI; HUMANS; INCLUSION BODIES; NERVE GROWTH FACTOR; PLASMIDS; PROTEIN FOLDING; PROTEIN PRECURSORS; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; ULTRACENTRIFUGATION;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0034851615     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2001.02232.x     Document Type: Article

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