Comparison of properties between human recombinant and placental copper-zinc SOD
| Autor: | Masahiko Yabuuchi, Mitsuo Enomoto, Kazuo Katoh, Jun-ichi Kajihara, Keiko Nishijima |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
Placenta
Molecular Sequence Data Mineralogy chemistry.chemical_element Zinc Biochemistry Peptide Mapping Superoxide dismutase Pregnancy Humans Amino Acid Sequence Molecular Biology Alanine Gel electrophoresis chemistry.chemical_classification biology Superoxide Dismutase Circular Dichroism Electron Spin Resonance Spectroscopy Active site General Medicine Recombinant Proteins Amino acid Isoelectric point Enzyme chemistry biology.protein Electrophoresis Polyacrylamide Gel Female Spectrophotometry Ultraviolet |
| Zdroj: | Journal of biochemistry. 104(5) |
| ISSN: | 0021-924X |
| Popis: | The physicochemical properties of purified recombinant human copper-zinc superoxide dismutase (r-hSOD) were compared with those of human placental copper-zinc superoxide dismutase (h-SOD). No differences were found in specific activity, metal contents, amino acid composition, and tryptic peptide map. The spectrophotometric properties including UV, ESR, and CD spectra were also similar. The result of isoelectric gel electrophoresis showed that the difference in isoelectric point (pI) was derived from acetylation of the N-terminal amino acid (alanine) in h-SOD. In SDS-polyacrylamide gel electrophoresis, both SODs showed the same behavior and enzymic activity was retained only under non-reducing conditions. ESR analysis of the denatured enzyme suggested that the high stability was derived from the structure of the active site around copper. Experiments using other metal-substituted SODs (Cu, Co in place of zinc) suggested that zinc contributed to the stability and the unique electrophoretic behavior of the enzyme. |
| Databáze: | OpenAIRE |
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