Biochemical properties of C78SC96S rhFGF-2: A double point-mutated rhFGF-2 increases obviously its activity

Journal of Biotechnology

Volumn 121, Issue 4, 2006, Pages 442-447

  Wang, Ju ^a   Hong, An ^a   Ren, Jin Song ^b   Sun, Fen Yong ^a   Shi, Ying Jiao ^a   Liu, Kan ^a   Xie, Qiu Ling ^a   Dai, Yun ^a   Li, Zhi Ying ^a   Chen, Yu ^c  

^a JINAN UNIVERSITY   (China)

^b CHANGCHUN INSTITUTE OF APPLIED CHEMISTRY   (China)

^c CHINESE UNIVERSITY OF HONG KONG   (Hong Kong)

Author keywords

Fluorescence spectroscopy; Mitogenic activity; Mutation; rhFGF 2

Indexed keywords

CELLS; ESCHERICHIA COLI; GENES; HYDROPHOBICITY; MUTAGENESIS; POLYPEPTIDES;

FLUORESCENCE SPECTROSCOPY; MITOGENIC ACTIVITY; MUTATION; RHFGF-2;

METABOLITES;

FIBROBLAST GROWTH FACTOR 2; FIBROBLAST GROWTH FACTOR RECEPTOR; RECOMBINANT HUMAN FIBROBLAST GROWTH FACTOR 2; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; BACTERIAL MUTATION; BACTERIUM MUTANT; BIOLOGICAL ACTIVITY; CELL INCLUSION; CELL STRAIN 3T3; CIRCULAR DICHROISM; DIMERIZATION; ESCHERICHIA COLI; FIBROBLAST; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY; MITOGENESIS; MOUSE; MUTANT; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; RECEPTOR AFFINITY; RECEPTOR BINDING; WILD TYPE;

3T3 CELLS; AMINO ACID SUBSTITUTION; ANIMALS; CELL PROLIFERATION; FIBROBLAST GROWTH FACTOR 2; HUMANS; MICE; POINT MUTATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

ANIMALIA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 32044474870     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2005.08.021     Document Type: Article

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