Inhibitory Monoclonal Antibody against Japanese Radish Acid Phosphatase

Ryoji Takata; Makoto Yoshimoto; Takahisa Miyamoto; Shoji Hatano; Jiro Sakamoto; Takahiko Soeda

doi:10.1271/bbb.57.1924

Inhibitory Monoclonal Antibody against Japanese Radish Acid Phosphatase

Ryoji Takata, Makoto Yoshimoto, Takahisa Miyamoto, Shoji Hatano, Jiro Sakamoto, Takahiko Soeda

Food Science and Biotechnology

Research output: Contribution to journal › Article

5 Citations (Scopus)

Abstract

Thirty stable hybridoma cell lines secreting monoclonal antibodies specific for Japanese radish acid phosphatase (EC 3.1.3.2) were obtained. These antibodies were inhibitory or stimulatory or had no effect on the enzyme activity. Four antibodies (IgG₁ subclass) among them, designated MAb-11, MAb-18, MAb-20, and MAb-30, were purified and partially characterized. MAb-11, MAb-18, and MAb-20 inhibited more than 80% of the enzyme activity and appeared to act as noncompetitive inhibitors. Competitive inhibition assay indicated that MAb-18 and MAb-20 were classified into the same group and MAb-11 into another group. MAb-20 had an inhibitory effect on acid phosphatases from some vegetable and meat sources. The Fab fragment prepared by limited proteolysis of MAb-20 with papain also inhibited the enzyme.

Original language	English
Pages (from-to)	1924-1928
Number of pages	5
Journal	Bioscience, Biotechnology, and Biochemistry
Volume	57
Issue number	11
DOIs	https://doi.org/10.1271/bbb.57.1924
Publication status	Published - Jan 1 1993

All Science Journal Classification (ASJC) codes

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

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Takata, R., Yoshimoto, M., Miyamoto, T., Hatano, S., Sakamoto, J., & Soeda, T. (1993). Inhibitory Monoclonal Antibody against Japanese Radish Acid Phosphatase. Bioscience, Biotechnology, and Biochemistry, 57(11), 1924-1928. https://doi.org/10.1271/bbb.57.1924

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abstract = "Thirty stable hybridoma cell lines secreting monoclonal antibodies specific for Japanese radish acid phosphatase (EC 3.1.3.2) were obtained. These antibodies were inhibitory or stimulatory or had no effect on the enzyme activity. Four antibodies (IgG1 subclass) among them, designated MAb-11, MAb-18, MAb-20, and MAb-30, were purified and partially characterized. MAb-11, MAb-18, and MAb-20 inhibited more than 80% of the enzyme activity and appeared to act as noncompetitive inhibitors. Competitive inhibition assay indicated that MAb-18 and MAb-20 were classified into the same group and MAb-11 into another group. MAb-20 had an inhibitory effect on acid phosphatases from some vegetable and meat sources. The Fab fragment prepared by limited proteolysis of MAb-20 with papain also inhibited the enzyme.",

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AU - Yoshimoto, Makoto

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AU - Soeda, Takahiko

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