Studies on mammalian intestinal peroxidase
| Autor: | S Kimura, P H Jellinck |
|---|---|
| Rok vydání: | 1982 |
| Předmět: |
Arginine
GPX3 Lysine Hydroxamic Acids Biochemistry Chromatography Affinity Intestine Small Animals Amino Acid Sequence Amino Acids Molecular Biology chemistry.chemical_classification biology Cytochrome c peroxidase Chemistry Guaiacol Lactoperoxidase Cell Biology Molecular biology Rats Amino acid Peroxidases Spectrophotometry Myeloperoxidase Chromatography Gel biology.protein Electrophoresis Polyacrylamide Gel Female Oxidation-Reduction Research Article Peroxidase |
| Zdroj: | Biochemical Journal. 205:271-279 |
| ISSN: | 0264-6021 |
| DOI: | 10.1042/bj2050271 |
| Popis: | A peroxidase, purified from rat small intestine to apparent homogeneity as judged by polyacrylamide-gel electrophoresis, exhibited an absorbance ratio (A412/A280) of 0.783. Its Mr (44000 +/- 1000) and spectral properties were similar to those of the pig intestinal enzyme. The velocity constant for the reaction between rat intestinal peroxidase and hydrogen peroxide was found to be 1.8×10(7) M-1 . s-1. Benzhydroxamic acid inhibited the peroxidative oxidation of guaiacol by intestinal peroxidase from both species but the concentration required to cause half-inhibition of the enzyme from the rat was higher by one order of magnitude than for the pig enzyme. The amino acid composition of highly-purified pig intestinal peroxidase showed a relative abundance of basic amino acids (lysine and arginine) and was similar to that of lactoperoxidase, but not that of myeloperoxidase. The initial ten amino acid residues of this enzyme (the first reported partial sequence for a mammalian peroxidase) were also determined. |
| Databáze: | OpenAIRE |
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