Recombinant proteins fused to thermostable partners can be purified by heat incubation

Journal of Biotechnology

Volumn 107, Issue 2, 2004, Pages 125-133

  De Marco, Ario ^a   Casatta, Elisabetta ^b   Savaresi, Sara ^a   Geerlof, Arie ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b UNIVERSITY OF UDINE   (Italy)

Author keywords

Expression vector; Heat incubation; Recombinant protein; Thermostability

Indexed keywords

BACTERIA; ENZYMES; ESCHERICHIA COLI; PRECIPITATION (CHEMICAL); PURIFICATION;

HEAT INCUBATION;

BIOTECHNOLOGY;

ESCHERICHIA COLI PROTEIN; FORMYLMETHANOFURAN:TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE; HYBRID PROTEIN; PROTEINASE; RECOMBINANT PROTEIN; TRANSFERASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME DEGRADATION; ESCHERICHIA COLI; EXPRESSION VECTOR; HEAT TREATMENT; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN IMMOBILIZATION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; PROTEIN TARGETING; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; THERMOSTABILITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; METHANOPYRUS KANDLERI; TOBACCO ETCH VIRUS;

EID: 0347985703     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2003.10.008     Document Type: Article

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