通过高碘酸根阴离子处理使脱辅基卵转铁蛋白中的酪氨酸残基发生交联。
The cross-linking of tyrosine residues in apo-ovotransferrin by treatment with periodate anions.
作者信息
Hsuan J J
机构信息
Department of Biochemistry, University of Bristol, U.K.
出版信息
Biochem J. 1987 Oct 15;247(2):467-73. doi: 10.1042/bj2470467.
Abstract
The iron-binding ability of apotransferrins is rapidly abolished in the reaction with periodate anions, which destroys 4 mol of tyrosine per mol of protein. Treatment of ovotransferrin with cyanogen bromide and tryptic digestion of the glycopeptide fragment demonstrated the existence of an intramolecular cross-link in the C-terminal domain of the oxidized protein. The cross-linked residues were identified as Tyr-421 and Tyr-524 and the product is similar in structure to 3,3'-dityrosine.
摘要
脱铁转铁蛋白与高碘酸根阴离子反应时，其铁结合能力迅速丧失，该反应每摩尔蛋白质会破坏4摩尔酪氨酸。用溴化氰处理卵转铁蛋白并对糖肽片段进行胰蛋白酶消化，结果表明氧化蛋白的C端结构域存在分子内交联。交联的残基被鉴定为Tyr-421和Tyr-524，产物的结构与3,3'-二酪氨酸相似。
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