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• W788325653 abstract "In this report we have analyzed interacting partners of hemoglobin inside erythrocyte and sought possible implications of hemoglobin-spectrin interaction. Our list of identified cytosolic hemoglobin interacting proteins includes redox regulators like peroxiredoxin-2, Cu-Zn superoxide dismutase, catalase, aldehyde dehydrogenase-1, flavin reductase and chaperones like HSP70, α-hemoglobin stabilizing protein. Others include metabolic enzymes like carbonic anhydrase-1, selenium binding protein-1, purine nucleoside phosphorylase and nucleoside diphosphate kinase. Additionally, various membrane proteins like α and β spectrin, ankyrin, band3, protein4.1, actin and glyceraldehyde 3 phosphate dehydrogenase have been shown to interact with hemoglobin. Our result indicates that major membrane skeleton protein spectrin, that also has a chaperone like activity, helps to fold the unstable alpha-globin chains in vitro. Taken together our results could provide insight into a protein network evolved around hemoglobin molecule inside erythrocyte that may add a new perspective in understanding the hemoglobin function and homeostasis." @default.
• W788325653 created "2016-06-24" @default.
• W788325653 creator A5054608319 @default.
• W788325653 creator A5091522212 @default.
• W788325653 date "2015-10-01" @default.
• W788325653 modified "2023-10-02" @default.
• W788325653 title "Hemoglobin interacting proteins and implications of spectrin hemoglobin interaction" @default.
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• W788325653 doi "https://doi.org/10.1016/j.jprot.2015.06.014" @default.
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