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2 results on '"Noriyoshi Kawashima"'

1. Efficient Peroxide Decoloration of C.I. Acid Orange 7 Catalyzed by Manganese Mesoporphyrin Dimer Derivatives in Micellar Solutions

Author

Noriyoshi Kawashima, Takehisa Dewa, Ryoko Umemura, Hiroyuki Mino, Syuichi Ishigure, Mamoru Nango, Shigeru Itoh, Masaharu Kondo, Shingo Ito, Keiji Yamashita, Tatsuro Mitsui, and Takafumi Hashimoto

Subjects
chemistry.chemical_compound, chemistry, Dimer, Micellar solutions, Organic chemistry, General Chemistry, Orange (colour), Hydrogen peroxide, C.I. Acid Orange, Peroxide, Catalysis, Manganese mesoporphyrin, Nuclear chemistry
Abstract

Manganese mesoporphyrin derivatives with hydrogen peroxide efficiently catalyzed the decoloration of C.I. Acid Orange 7 in micellar solutions under mild conditions such as pH 8.0 and 25 °C. The max...

Published
2005
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2. Anti-erythropoietin receptor monoclonal antibody: epitope mapping, quantification of the soluble receptor, and detection of the solubilized transmembrane receptor and the receptor-expressing cells

Author

Emi Morishita, Masaya Nagao, Noriyoshi Kawashima, Hajime Hatta, Seiji Masuda, Kenji Yamagishi, Hiroshi Narita, Ryuzo Sasaki, and Motoyuki Nishida

Subjects
medicine.drug_class, Immunology, Blotting, Western, Molecular Sequence Data, Enzyme-Linked Immunosorbent Assay, Nerve Tissue Proteins, Biology, Monoclonal antibody, Biochemistry, Hippocampus, PC12 Cells, Epitope, Cell Line, Epitopes, Mice, Species Specificity, Cell surface receptor, medicine, Receptors, Erythropoietin, Animals, Humans, Amino Acid Sequence, Receptor, Peptide sequence, Neurons, Hybridomas, Sequence Homology, Amino Acid, food and beverages, Antibodies, Monoclonal, Cell Biology, Hematology, Molecular biology, Erythropoietin receptor, Rats, Epitope mapping, Ectodomain, Solubility, embryonic structures, Sequence Alignment
Abstract

A hybridoma cell line producing the monoclonal antibody against erythropoietin receptor (EpoR) was established using the soluble ectodomain of mouse erythropoietin receptor (sEpoR) as an antigen. The monoclonal antibody termed 1G3 bound to the denatured sEpoR. Epitope mapping with peptide library revealed that 1G3 recognized the amino terminal region including the hexapeptide (positions 6 to 11; LeuProAspProLysPhe). The amino acid sequence in this hexapeptide was identical in mice, rats, and humans, and therefore 1G3 bound to EpoR from all of these sources. Using 1G3, we evaluated sEpoR by a sandwich enzyme-linked immunoassay, and EpoR in the solubilized membrane preparation was detected by Western blotting. The cells expressing EpoR were identified with immunochemical staining. We confirmed the presence of EpoR in a neuronal cell line and PC12 cells, and EpoR was expressed in primary cultured hippocampal neurons.

Published
1996

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