Optimal fusion of antibody binding domains resulted in higher affinity and wider specificity

Journal of Bioscience and Bioengineering

Volumn 120, Issue 5, 2015, Pages 504-509

  Dong, Jinhua ^a   Kojima, Tomoki ^b   Ohashi, Hiroyuki ^b,c   Ueda, Hiroshi ^a  

^a TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c USHIO INC   (Japan)

Author keywords

Affinity tag; Antibody binding protein; Avidity effect; Immunoassay; Linker engineering

Indexed keywords

ANTIGENS; BINDING SITES; COST EFFECTIVENESS; MAMMALS; PROTEINS; PURIFICATION;

AFFINITY TAG; ANTIBODY BINDING; AVIDITY EFFECT; BIOMEDICAL FIELDS; IMMUNOASSAY; INTERCHAIN DISTANCES; NATURAL PROTEINS; POSSIBLE MECHANISMS;

ANTIBODIES;

ANTIBODY; BACTERIAL PROTEIN; BINDING PROTEIN; FUSION PROTEIN PAXPG; HYBRID PROTEIN; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G; IMMUNOGLOBULIN HEAVY CHAIN; LINK PROTEIN; STAPHYLOCOCCUS PROTEIN A; STREPTOCOCCUS PROTEIN G; UNCLASSIFIED DRUG; IGG FC-BINDING PROTEIN, STREPTOCOCCUS;

ANTIBODY COMBINING SITE; ANTIBODY SPECIFICITY; ANTIGEN BINDING; ARTICLE; BINDING AFFINITY; HUMAN; MOLECULAR MODEL; MOLECULAR SIZE; MOUSE; NONHUMAN; PROTEIN BINDING; PROTEIN DETERMINATION; PROTEIN DOMAIN; PROTEIN PURIFICATION; PROTEIN STRUCTURE; ANIMAL; ANTIBODY AFFINITY; BINDING SITE; CHEMISTRY; IMMUNOLOGY; PLIABILITY; PROTEIN TERTIARY STRUCTURE;

ANIMALS; ANTIBODY AFFINITY; ANTIBODY SPECIFICITY; BACTERIAL PROTEINS; BINDING SITES; HUMANS; IMMUNOGLOBULIN FAB FRAGMENTS; IMMUNOGLOBULIN FC FRAGMENTS; IMMUNOGLOBULIN G; MICE; PLIABILITY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; STAPHYLOCOCCAL PROTEIN A;

EID: 84943362455     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2015.03.014     Document Type: Article

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