作者: Robert L. Perlman , Harold Edelhoch
DOI: 10.1016/S0021-9258(18)95977-6
关键词: Human serum albumin 、 Iodine 、 Chemistry 、 Urea 、 Chromatography 、 Diiodotyrosine 、 Cell biology 、 Biochemistry 、 Molecular biology
摘要: Abstract Human serum albumin (HSA) has been allowed to react with varying amounts of iodine under mild conditions. Almost all the tyrosyl residues HSA may be converted iodotyrosyl (primarily diiodotyrosyl) without producing significant changes in conformation protein. Difference spectral measurements urea show disappearance "buried" and appearance diiodotyrosyl residues; a difference peak attributed iodinated is seen at 302 mµ. It proposed that partly nonaqueous environment directs their preferential conversion residues.