Subcellular Localization of Beta Hemoglobin Using pSNAPf fusion Protein

Abstract: Much of what is known about hemoglobin relates to its structure and function. However, there is a great deal to learn about its assembly. The application of new technologies has allowed us to investigate the process of hemoglobin synthesis extensively. It has been shown that heme, synthesized in the mitochondria, is exported into the cytoplasm where it rapidly binds with apoglobin synthesized by polyribosomes. In this study,subcellular localization of newly synthesized alpha and beta subunits of human hemoglobin were examined using fluorescence microscopic imaging of cultured human erythroleukemic cells (cell line HEL 92.1.7). Experiments were used to determine the location of newly synthesized protein subunits. This paper will highlight the current knowledge of hemoglobin assembly, function and cellular interactions; and illustrate how cellular labels can be used to investigate this protein. It is hoped that future experiments will help to determine more details of the mechanism of globin assembly, which will be useful in the investigation of hemoglobinopathies. Disclosures No relevant conflicts of interest to declare.