Fusion of the antiferritin antibody VL domain to barnase results in enhanced solubility and altered pH stability

Protein Engineering, Design and Selection

Volumn 17, Issue 1, 2004, Pages 85-93

  Martsev, Sergey P ^a   Tsybovsky, Yaroslav I ^a   Stremovskiy, Oleg A ^b   Odintsov, Sergey G ^a   Balandin, Taras G ^b   Arosio, Paolo ^c   Kravchuk, Zinaida I ^a   Deyev, Sergey M ^b  

^a INSTITUTE OF BIOORGANIC CHEMISTRY   (Belarus)

^b SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

^c UNIVERSITY OF BRESCIA   (Italy)

Author keywords

Chaperone like function; Immunotoxin; Protein stability; RNase; VL domain

Indexed keywords

BARNASE; FERRITIN ANTIBODY; HYBRID PROTEIN; ISOFERRITIN; RIBONUCLEASE;

AMINO TERMINAL SEQUENCE; ANTIBODY AFFINITY; ANTIBODY SPECIFICITY; ANTIGEN BINDING; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL INCLUSION; CHIMERA; CONTROLLED STUDY; CYTOPLASM; CYTOTOXICITY; DIMERIZATION; ENZYME ACTIVITY; ESCHERICHIA COLI; FLUORESCENCE; GEL PERMEATION CHROMATOGRAPHY; IMMUNOGLOBULIN VARIABLE REGION; IN VITRO STUDY; IN VIVO STUDY; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; SOLUBILITY;

AMINO ACID SEQUENCE; ANTIBODIES; CHROMATOGRAPHY; CHROMATOGRAPHY, GEL; CYTOPLASM; DIMERIZATION; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; FERRITINS; HYDROGEN-ION CONCENTRATION; IMMUNOGLOBULIN VARIABLE REGION; MOLECULAR SEQUENCE DATA; PLASMIDS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; RIBONUCLEASES; SOLUBILITY; SPECTROMETRY, FLUORESCENCE;

BACILLUS AMYLOLIQUEFACIENS; ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0842313319     PISSN: 17410126     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/gzh011     Document Type: Article

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