Switching an anti-IgG binding site between archaeal extremophilic proteins results in Affitins with enhanced pH stability

Journal of Biotechnology

Volumn 192, Issue Part A, 2014, Pages 123-129

  Béhar, Ghislaine ^a,b   Pacheco, Sabino ^a,b   Maillasson, Mike ^a,b,c   Mouratou, Barbara ^a,b   Pecorari, Frédéric ^a,b  

^a Team 12   (France)

^b UNIVERSITÉ DE NANTES   (France)

^c Plate forme IMPACT Biogenouest   (France)

Author keywords

Affitin; Molecular grafting; PH stability; Sac7d; Sso7d; Thermostability

Indexed keywords

ALKALINITY; BIOTECHNOLOGY; ESCHERICHIA COLI; PROTEINS; SCAFFOLDS (BIOLOGY); STABILITY; THERMODYNAMIC STABILITY;

AFFITIN; MOLECULAR GRAFTING; PH STABILITY; SAC7D; SSO7D; THERMOSTABILITY;

PH EFFECTS;

ARCHAEAL PROTEIN; IMMUNOGLOBULIN G ANTIBODY; SCAFFOLD PROTEIN; ANTI-IGG; ANTIIDIOTYPIC ANTIBODY; DNA BINDING PROTEIN; IMMUNOGLOBULIN G;

ALKALINITY; ANTIBODY COMBINING SITE; ARTICLE; BACTERIAL MUTATION; CHIMERA; CONTROLLED STUDY; DNA SEQUENCE; ESCHERICHIA COLI; GENE SWITCHING; NONHUMAN; THERMOSTABILITY; WILD TYPE; BINDING SITE; GENETICS; HEAT; METABOLISM; MUTATION; PH; PROTEIN ENGINEERING;

ANTIBODIES, ANTI-IDIOTYPIC; ARCHAEAL PROTEINS; BINDING SITES; DNA-BINDING PROTEINS; ESCHERICHIA COLI; HOT TEMPERATURE; HYDROGEN-ION CONCENTRATION; IMMUNOGLOBULIN G; MUTATION; PROTEIN ENGINEERING;

EID: 84909582000     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2014.10.006     Document Type: Article

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