Rapid proteolysis of puromycyl peptides in non-thalassaemic and thalassaemic erythroid cells
| Autor: | G. Chalevelakis, Cosmas Lyberatos, Sotirios A. Raptis, Athanasios Yalouris, Emmanuel Vaidakis, George Pallikaris |
|---|---|
| Rok vydání: | 1984 |
| Předmět: |
Erythroblasts
Proteolysis Clinical Biochemistry Bone Marrow Cells Proteolytic degradation Peptide Biology Tritium Biochemistry medicine Humans Beta (finance) chemistry.chemical_classification medicine.diagnostic_test Hydrolysis Heterozygote advantage General Medicine Molecular biology Peripheral blood Beta-thalassaemia medicine.anatomical_structure chemistry Thalassemia Puromycin Bone marrow Peptides Half-Life |
| Zdroj: | European Journal of Clinical Investigation. 14:199-202 |
| ISSN: | 1365-2362 0014-2972 |
| DOI: | 10.1111/j.1365-2362.1984.tb01123.x |
| Popis: | The proteolytic degradation of labelled pyromycyl polypeptides was investigated in human intact erythroid cells derived from the bone marrow of eight non-thalassaemic patients and the peripheral blood of eleven thalassaemics (eight splenectomized beta thalassaemia heterozygotes and three sickle-cell beta thalassaemics). These abnormal polypeptides are rapidly degraded to soluble trichloroacetic-acid (TCA) fragments with a half-life of 12 min both in bone marrow and peripheral blood. This comes very close to the half-life reported for the puromycyl peptide degradative system in rabbit reticulocytes (15 min). The relationship of the present proteolytic system to the ATP-dependent one, described in rabbit reticulocytes, and to that responsible for the free alpha-chain degradation in beta thalassaemia is discussed. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text