Alteration of Antigen Recognition by Anti-Hapten Antibody during Affinity Maturation.
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Accession number;01A0903150
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| Title;Alteration of Antigen Recognition by Anti-Hapten Antibody during Affinity Maturation. |
| Author;
ODA MASAYUKI
(Sci. Univ. Tokyo, Res. Inst. Biological Sci., JPN)
SAGAWA TAKUMA
(Sci. Univ. Tokyo, Res. Inst. Biological Sci., JPN)
ISHIMURA MIYUKI
(Natl. Inst. of Bioscience and Human-Technol. Agency of Ind. Sci. and Technol.)
MORII HISAYUKI
(Natl. Inst. of Bioscience and Human-Technol. Agency of Ind. Sci. and Technol.)
FURUKAWA KOJI
(Sci. Univ. Tokyo, Res. Inst. Biological Sci., JPN)
AZUMA TAKACHIKA
(Sci. Univ. Tokyo, Res. Inst. Biological Sci., JPN)
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Journal Title;Netsu Sokutei Toronkai Koen Yoshishu
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Journal Code:F0840B
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ISSN:
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VOL.36th;NO.;PAGE.26-27(2000)
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| Figure&Table&Reference;REF.9 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;Antibodies(Abs) have long been considered an excellent biological reagent for medical treatment or analysis, and high affinity Abs were required for such purpose. The amino acid substitution of Abs, caused by somatic mutation, creates a variability for antigen(Ag) recognition that can be used for affinity improvements. Affinity of anti-(4-hydroxy-3-nitrophenyl)aetyl(NP) Abs to NP increased with time after immunization over 1,000-fold. In order to understand the mechanism of affinity maturation, we examined the Ag-Ab interactions by isothermal titration calorimetry and surface plasmon resonance biosensor. Four kinds of Abs, arose from the same ancestral clone, were matured with a decrease in the negative entropy change. The SPR experiments showed that the mature Ab has slower association and dissociation rate constants. The most plausible explanation of these results is that somatic mutation can stabilize the coniguration of the combining site and Ag binds to mature Ab by a lock-and-key fit mechanism. (author abst.) |
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