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 | |
| Publication status | Published - Jan 1 1993 |
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All Science Journal Classification (ASJC) codes
- Biotechnology
- Analytical Chemistry
- Biochemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry
Cite this
Inhibitory Monoclonal Antibody against Japanese Radish Acid Phosphatase. / Takata, Ryoji; Yoshimoto, Makoto; Miyamoto, Takahisa; Hatano, Shoji; Sakamoto, Jiro; Soeda, Takahiko.
In: Bioscience, Biotechnology, and Biochemistry, Vol. 57, No. 11, 01.01.1993, p. 1924-1928.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Inhibitory Monoclonal Antibody against Japanese Radish Acid Phosphatase
AU - Takata, Ryoji
AU - Yoshimoto, Makoto
AU - Miyamoto, Takahisa
AU - Hatano, Shoji
AU - Sakamoto, Jiro
AU - Soeda, Takahiko
PY - 1993/1/1
Y1 - 1993/1/1
N2 - 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.
AB - 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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UR - http://www.scopus.com/inward/citedby.url?scp=85007799822&partnerID=8YFLogxK
U2 - 10.1271/bbb.57.1924
DO - 10.1271/bbb.57.1924
M3 - Article
VL - 57
SP - 1924
EP - 1928
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
SN - 0916-8451
IS - 11
ER -