Structure and synthesis of hemoglobin in marmosets (Saguinus fuscicollis).
Marmoset reticulocytes and bone marrow provide a valuable tissue resource for the study of primate hemoglobin structure and synthesis. The amino acid sequence of the marmoset hemoglobin has been determined, and the close homology between it and that of the human suggest it may be a valuable model for study of the effects of chemical modification on hemoglobin function. Hemoglobin synthesis by fetal bone marrow has been reported to be stimulated by physiologic levels of l-thyroxine. Differences in hormone responsiveness between fetal and adult red cell precursors have tentatively been ascribed to differences in permeability of the fetal and adult clones of cells.
D000596:Amino Acids / Q000097:blood; D000818:Animals; D001853:Bone Marrow / Q000502:physiology; D002143:Callitrichinae / Q000097:blood*; D055598:Chemical Phenomena; D002621:Chemistry; D005319:Fetal Hemoglobin / Q000096:biosynthesis; D005914:Globins / Q000096:biosynthesis; D000882:Haplorhini; D006454:Hemoglobins / Q000096:biosynthesis*; D008954:Models, Biological; D012156:Reticulocytes / Q000502:physiology; D013974:Thyroxine / Q000502:physiology
D000596:Amino Acids; D006454:Hemoglobins; D005914:Globins; D005319:Fetal Hemoglobin; D013974:Thyroxine