Study of ferritin self-assembly and heteropolymer formation by the use of Fluorescence Resonance Energy Transfer (FRET) technology

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• 作者：Fernando Carmona^a ; Maura Poli^a ; Michela Bertuzzi^b ; Alessandra Gianoncelli^b ; Fabrizio Gangemi^c ; Paolo Arosio^a ; ^{paolo.arosio@unibs.it}
• 关键词：FTH ; homopolymer of human ferritin H-chains ; FTL ; homopolymer of human ferritin L-chains ; FTHL ; heteropolymer of human H- and L-chains ; FTMT ; homopolymer of human mitochondrial chains ; AF ; alexa fluor ; FTH-488 ; full-labeled FTH with AF488 ; FTH-555 ; full-labeled FTH with AF555 ; FTL-555 ; full labeled FTL with AF555 ; H-488 ; H-chain labeled with AF488 ; H-555 ; H-chain labeled with AF555 ; L-555 ; L-chain labeled with AF555 ; FRET ; fluorescence resonance energy transfer ; PAGE ; polyacrylamide gel electrop
• 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：1861
• 期：3
• 页码：522-532
• 全文大小：1610 K
• 卷排序：1861

文摘

A FRET-based approach to characterize human ferritin self-assembly is described. Self-assembly kinetics of H/L heteropolymers are faster than for H/H homopolymers. Heterodimeric (H/L) association is preferred during H/L heteropolymers formation. H-chains arrange preferentially at distant sites on H/L heteropolymeric shells.