Science Links Japan | Functional alteration of an antibody with the desired specificity and the precise analyses of engineered antibody-target antigen interactions.

Functional alteration of an antibody with the desired specificity and the precise analyses of engineered antibody-target antigen interactions.

Accession number;01A0228946

Title;Functional alteration of an antibody with the desired specificity and the precise analyses of engineered antibody-target antigen interactions.

Author; TSUMOTO KOHEI (Tohoku Univ., Grad. Sch.) NISHIMIYA YOSHIYUKI (Tohoku Univ., Grad. Sch.) SHIROISHI MITSUNORI (Tohoku Univ., Grad. Sch.) KONDO HIDEMASA (Hokkaido National Ind. Res. Inst.) KUMAGAI IZUMI (Tohoku Univ., Grad. Sch.)

Journal Title;Abstracts. Symposium on Biofunctional Chemistry

Journal Code:L0836A

ISSN:

VOL.15th;NO.;PAGE.8-9(2000)

Figure&Table&Reference;TBL.1, REF.5

Pub. Country;Japan

Language;Japanese

Abstract;Grafting high affinity toward mutated antigen onto anti-hen lysozyme (HEL) antibody HyHEL-10 has been achieved by saturation mutagenesis into four residues followed by selection with affinity for the target (TEL). Thermodynamic and structural analyses have demonstrated that not only local complementarity of antigen-antibody interface but also VL-VH interaction make significant contribution to the enhancement of antibody affinity for target antigens. (author abst.)

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