Some physical and immunological properties of ox kidney biliverdin reductase
| Autor: | E. M. Rigney, Timothy J. Mantle, Orla M. Phillips |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
Oxidoreductases Acting on CH-CH Group Donors
Immunoblotting Hamster Dithionitrobenzoic Acid Kidney Biochemistry Immunoenzyme Techniques chemistry.chemical_compound Cytosol Species Specificity polycyclic compounds medicine Animals Humans Tissue Distribution Molecular Biology chemistry.chemical_classification Antiserum Aldose reductase Binding Sites Biliverdin Biliverdin reductase Cell Biology Glutathione Rats Enzyme medicine.anatomical_structure chemistry Cattle Electrophoresis Polyacrylamide Gel Isoelectric Focusing Oxidoreductases Research Article |
| Zdroj: | Biochemical Journal. 255:431-435 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj2550431 |
| Popis: | The liver, kidney and spleen of the mouse and rat and the kidney and spleen of the ox express a monomeric form of biliverdin reductase (Mr 34,000), which in the case of the ox kidney enzyme exists in two forms (pI 5.4 and 5.2) that are probably charge isomers. The livers of the mouse and rats express, in addition, a protein (Mr 46,000) that cross-reacts with antibodies raised against the ox kidney enzyme and may be related to form 2 described by Frydman, Tomaro, Awruch & Frydman [(1983) Biochim. Biophys. Acta 759, 257-263]. Higher-Mr forms appear to exist in the guinea pig and hamster. The ox kidney enzyme has three thiol groups, of which two are accessible to 5,5′-dithiobis-(2-nitrobenzoate) in the native enzyme. Immunocytochemical analysis reveals that biliverdin reductase is localized in proximal tubules of the inner cortex of the rat kidney. Biliverdin reductase antiserum also stains proximal tubules in human and ox kidney. The staining of podocytes in glomeruli of ox kidney with antiserum to aldose reductase is particularly prominent. The localization of biliverdin reductase in the inner cortical zone of rat kidney is similar to that described for glutathione S-transferase YfYf, and it is suggested that one function of this ‘intracellular binding protein’ may be to maintain a low free concentration of biliverdin to allow biliverdin reductase to operate efficiently. |
| Databáze: | OpenAIRE |
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