pTo produce functional Hb (haemoglobin), nascent α-globin (αsupo/sup) and β-globin (βsupo/sup) chains must each bind a single haem molecule (to form αsuph/sup and βsuph/sup) and interact together to form heterodimers. The precise sequence of binding events is unknown, and it has been suggested that additional factors might enhance the efficiency of Hb folding. AHSP (α-haemoglobin-stabilizing protein) has been shown previously to bind αsuph/sup and regulate redox activity of the haem iron. In the present study, we used a combination of classical and dynamic light scattering and NMR spectroscopy to demonstrate that AHSP forms a heterodimeric complex with αsupo/sup that inhibits αsupo/sup aggregation and promotes αsupo/sup folding in the absence of haem. These findings indicate that AHSP may function as an αsupo/sup-specific chaperone, and suggest an important role for αsupo/sup in guiding Hb assembly by stabilizing βsupo/sup and inhibiting off-pathway self-association of βsuph/sup./p
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机译：>要产生功能性Hb（血红蛋白），新生的α-球蛋白（α o ）和β-球蛋白（β o ）链必须分别结合一个血红素分子（形成α h 和β h ）并相互作用形成异二聚体。结合事件的确切顺序是未知的，并且已经提出其他因素可能会增强Hb折叠的效率。先前已证明AHSP（α血红蛋白稳定蛋白）可结合α h 并调节血红素铁的氧化还原活性。在本研究中，我们将经典光散射和动态光散射以及NMR光谱结合使用，证明AHSP与α o 形成异二聚体复合物，从而抑制α o 聚集并促进在没有血红素的情况下，α o 折叠。这些发现表明，AHSP可能作为α o 特异性伴侣分子起作用，并暗示α o 通过稳定β o 在引导Hb组装中起重要作用。 sup>和抑制β h 的路径外缔合。
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