Heating as a rapid purification method for recovering correctly-folded thermotolerant VH and VHH domains

BMC Biotechnology

Volumn 7, Issue , 2007, Pages

  Olichon, Aurelien ^a   Schweizer, Daniel ^a   Muyldermans, Serge ^b   de Marco, Ario ^a,c  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^c Biochemistry Unit   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

CAMELIDAE (VHHS); HEAT TOLERANCE; HEAT-INDUCED DENATURATION; RE-FOLDING CAPABILITY; THERMOTOLERANT PROTEINS;

AFFINITY CHROMATOGRAPHY; ANTIBODIES; BIOTECHNOLOGY; PROTEINS; PURIFICATION;

HEAT TREATMENT;

BACTERIAL PROTEIN; RECOMBINANT ANTIBODY; RECOMBINANT PROTEIN;

AFFINITY CHROMATOGRAPHY; ARTICLE; CAMEL; DENATURATION; HEAT TOLERANCE; HEAT TREATMENT; HEATING; NONHUMAN; PRECIPITATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; TEMPERATURE;

ANIMALS; ANTIBODIES, MONOCLONAL; CAMELIDS, NEW WORLD; CHEMICAL FRACTIONATION; HOT TEMPERATURE; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY;

BACTERIA (MICROORGANISMS); CAMELIDAE;

EID: 33846979756     PISSN: None     EISSN: 14726750     Source Type: Journal    
DOI: 10.1186/1472-6750-7-7     Document Type: Article

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