Bisphosphoglycerate synthase activity in cells of the erythrocytic line of rat.
The specific activity of bisphosphoglycerate synthase (EC 2.7.5.4) is significantly higher in rat mature erythrocytes than in reticulocytes from phenylhydrazine treated animals, while 2,3-bisphosphoglycerate levels do not differ between them. The enzyme specific activity and the concentration of 2,3-bisphosphoglycerate are both negligible in the erythroid cell pool from the bone marrow of anaemic animals. Thus, a cellular specialization in the last stages of erythropoiesis is confirmed. Human bisphosphoglycerate synthase shows a lower specific activity than that of rat without a parallel decrease in 2,3-bisphosphoglycerate levels.
D019794:2,3-Diphosphoglycerate; D000740:Anemia / Q000097:blood / Q000201:enzymology; D000818:Animals; D001731:Bisphosphoglycerate Mutase / Q000097:blood*; D001853:Bone Marrow / Q000201:enzymology; D004163:Diphosphoglyceric Acids / Q000097:blood*; D004912:Erythrocytes / Q000201:enzymology*; D004920:Erythropoiesis; D006454:Hemoglobins / Q000032:analysis; D006801:Humans; D010659:Phenylhydrazines; D010770:Phosphotransferases / Q000097:blood*; D051381:Rats; D011919:Rats, Inbred Strains; D012156:Reticulocytes / Q000201:enzymology*
D004163:Diphosphoglyceric Acids; D006454:Hemoglobins; D010659:Phenylhydrazines; D019794:2,3-Diphosphoglycerate; D010770:Phosphotransferases; D001731:Bisphosphoglycerate Mutase