Rapid proteolysis of puromycyl peptides in non-thalassaemic and thalassaemic erythroid cells.
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.
D001854:Bone Marrow Cells; D004900:Erythroblasts / Q000378:metabolism*; D006207:Half-Life; D006801:Humans; D006868:Hydrolysis; D010455:Peptides / Q000378:metabolism*; D011691:Puromycin / Q000378:metabolism*; D013789:Thalassemia / Q000097:blood / Q000473:pathology*; D014316:Tritium
D010455:Peptides; D014316:Tritium; D011691:Puromycin