Purification and subunit structure of argininosuccinate lyase from Chlamydomonas reinhardi
| Autor: | J P Schlösser, R F Matagne |
|---|---|
| Rok vydání: | 1977 |
| Předmět: |
Macromolecular Substances
Protein subunit Size-exclusion chromatography Lyases Biology Biochemistry chemistry.chemical_compound Molecular Biology Polyacrylamide gel electrophoresis Mercaptoethanol chemistry.chemical_classification Chromatography Chlamydomonas Cell Biology Argininosuccinate lyase Argininosuccinate Lyase Enzyme assay Molecular Weight Enzyme chemistry Sephadex Acrylamide biology.protein Chromatography Gel Electrophoresis Polyacrylamide Gel Research Article |
| Zdroj: | The Biochemical journal. 167(1) |
| ISSN: | 0264-6021 |
| Popis: | Argininosuccinate lyase (EC 4.3.2.1) was purified by (NH4)2SO4 fractionation, chromatography on DEAE-cellulose and gel filtration on Sephadex G-200. The final enzyme preparation was purified 46-fold compared with the crude extract. Electrophoresis of this preparation revealed three bands, the major one having the enzyme activity. Analysis of the enzyme by gel filtration and by disc electrophoresis (in two different concentrations of acrylamide) gave mol.wts. of 200000 (+/- 15000) and 190000 (+/- 20000) respectively. Treatment with sodium dodecyl sulphate and mercaptoethanol dissociated the enzyme into subunits of mol.wt. 39000 (+/-2000). The results are indicative of the multimeric structure of the enzyme, which is composed of five (perhaps four or six) identical subunits. |
| Databáze: | OpenAIRE |
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