Purification and Characterization of Rice Peroxidases
| Autor: | Akira Ohbayashi, Hiroyuki Ito, Nobutsugu Hiraoka, Yuko Ohashi |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Molecular Sequence Data
General Biochemistry Genetics and Molecular Biology Diffusion Drug Stability Sequence Homology Nucleic Acid Amino Acid Sequence Isoelectric Point Plant Proteins chemistry.chemical_classification Base Composition Oryza sativa biology Molecular mass Base Sequence Isoelectric focusing Temperature Oryza Hydrogen-Ion Concentration Ouchterlony double immunodiffusion Amino acid Enzyme Isoelectric point Biochemistry chemistry Peroxidases biology.protein General Agricultural and Biological Sciences Peroxidase |
| Zdroj: | Agricultural and Biological Chemistry. 55:2445-2454 |
| ISSN: | 1881-1280 0002-1369 |
| DOI: | 10.1271/bbb1961.55.2445 |
| Popis: | Four peroxidase components, named RP-2, 4, 6, and 7, were isolated from rice (Oryza sativa L.) green leaves. Isoelectric focusing indicated that each preparation was homogeneous. The molecular weights of RP-2, 4, 6, and 7 estimated by SDS-PAGE were 48,000, 48,000, 40,000, and 39,500, and their isoelectric points were 5.4, 8.1, 9.3, and 9.2, respectively. The activity of every preparation was maximum around pH 5.0. Antisera against these purified enzymes were raised in rabbits. Ouchterlony double diffusion tests with these antisera suggested that RP-6 and 7 were immunochemically identical and RP-2 and 4 were identical in parts and that RP-6 and 7 were quite different from RP-2 and 4. Analysis of the N-terminal amino acid sequences also showed that these peroxidase components were classified into two groups. The polymerase chain reaction showed that RP-2 and/or RP-4 contained an active central region, which is homologous to other plant peroxidases. |
| Databáze: | OpenAIRE |
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