Subunits of the extracellular hemoglobin of Tubifex tubifex
| Autor: | Charles E. Frohman, Shannon L. Hersey, Oscar H. Kapp, Serge N. Vinogradov |
|---|---|
| Rok vydání: | 1979 |
| Předmět: |
biology
Macromolecular Substances Protein subunit biology.organism_classification Guanidines Biochemistry Genetics and Molecular Biology (miscellaneous) Tubifex Molecular biology Molecular Weight Hemoglobins chemistry.chemical_compound chemistry Biochemistry Tubifex tubifex Chromatography Gel Extracellular Electrophoresis Polyacrylamide Gel Hemoglobin Oligochaeta Sodium dodecyl sulfate Extracellular Space Guanidine Polyacrylamide gel electrophoresis |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure. 578:216-222 |
| ISSN: | 0005-2795 |
| DOI: | 10.1016/0005-2795(79)90129-6 |
| Popis: | The molecular weight of the extracellular hemoglobin of Tubifex tubifex determined by equilibrium sedimentation is 3.0 +/- 0.2 . 10(6). Polyacrylamide gel electrophoresis in sodium dodecyl sulfate showed that the hemoglobin dissociated into four subunits: 13 000 (subunit 1), 21 000 (subunit 2), 23 000 (subunit 3) and 47 000 (subunit 4); in the presence of mercaptoethanol two subunits were observed, 13 000 +/- 1000 (subunit I) accounting for 70--80% of the whole molecule, and 26 000 (subunit II). Electrophoresis of the subunits obtained in the absence of mercaptoethanol showed that subunit I originated from subunits 1 and 4, while subunit II originated from subunits 2 and 3. These relationships were supported by N-terminal group determinations. Gel filtration in 6 M guanidine hydrochloride showed that the molecular weight of subunit I is 17 500 and that of subunit II, 36 000. Tubifex hemoglobin appears to consist of at least seven polypeptide chains. |
| Databáze: | OpenAIRE |
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