Characterization of monoclonal antibodies to chitinase A1 and enhancement of chitinase A1 activity by monoclonal antibodies

Sakari Sekine, Yashushi Ito, Masayuki Hashimoto, Hirosato Tanaka, Takeshi Watanabe

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

A total of eleven hybridomas which secrete antibodies against chitinase A1 were established. Among the eleven monoclonal antibodies (MAbs) obtained, six recognized the catalytic domain, three recognized the type III region and two recognized the chitin binding domain of chitinase A1. Of the two MAbs which recognized the chitin binding domain one was found to also react with chitinase D, but none of the other MAbs which recognized either the type III region or the chitin binding domain reacted with chitinase D despite the extensive amino acid sequence similarity between both the type III and chitin binding domains of the two chitinases. Two of the eleven MAbs enhanced chitinase activity significantly, while the other MAbs did not have any significant effect on chitinase A1 activity.

Original languageEnglish
Pages (from-to)7-16
Number of pages10
JournalBiochemical and Biophysical Research Communications
Volume204
Issue number1
DOIs
Publication statusPublished - 1994 Oct 15

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Chitinases
Monoclonal Antibodies
Chitin
Hybridomas
Amino Acid Sequence
Catalytic Domain
Amino Acids
Antibodies

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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abstract = "A total of eleven hybridomas which secrete antibodies against chitinase A1 were established. Among the eleven monoclonal antibodies (MAbs) obtained, six recognized the catalytic domain, three recognized the type III region and two recognized the chitin binding domain of chitinase A1. Of the two MAbs which recognized the chitin binding domain one was found to also react with chitinase D, but none of the other MAbs which recognized either the type III region or the chitin binding domain reacted with chitinase D despite the extensive amino acid sequence similarity between both the type III and chitin binding domains of the two chitinases. Two of the eleven MAbs enhanced chitinase activity significantly, while the other MAbs did not have any significant effect on chitinase A1 activity.",
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Characterization of monoclonal antibodies to chitinase A1 and enhancement of chitinase A1 activity by monoclonal antibodies. / Sekine, Sakari; Ito, Yashushi; Hashimoto, Masayuki; Tanaka, Hirosato; Watanabe, Takeshi.

In: Biochemical and Biophysical Research Communications, Vol. 204, No. 1, 15.10.1994, p. 7-16.

Research output: Contribution to journalArticle

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AU - Sekine, Sakari

AU - Ito, Yashushi

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AU - Tanaka, Hirosato

AU - Watanabe, Takeshi

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