在胆红素和L-色氨酸主要结合位点研究中对人血清白蛋白进行丹磺酰化。
Dansylation of human serum albumin in the study of the primary binding sites of bilirubin and L-tryptophan.
作者信息
Jacobsen C, Jacobsen J
出版信息
Biochem J. 1979 Jul 1;181(1):251-3. doi: 10.1042/bj1810251.
Abstract
Binding of bilirubin and of L-tryptophan to dansylated albumins was investigated. Dansylation of less than one lysine residue per molecule of albumin did not affect the bilirubin binding, but decreased the L-tryptophan binding, indicating that dansylation had taken place in or near the l-tryptophan-binding site. Native albumin and albumin-bilirubin 1:1 complex showed the same affinity for L-tryptophan. The results indicate that, although L-tryptophan and bilirubin are bound in the same region, perhaps in a common cavity of the albumin molecule, such a cavity is sufficiently large to contain both ligands.
摘要
研究了胆红素和L-色氨酸与丹磺酰化白蛋白的结合情况。每分子白蛋白中少于一个赖氨酸残基的丹磺酰化不影响胆红素结合，但降低了L-色氨酸结合，这表明丹磺酰化发生在L-色氨酸结合位点内或其附近。天然白蛋白和白蛋白-胆红素1:1复合物对L-色氨酸表现出相同的亲和力。结果表明，虽然L-色氨酸和胆红素结合在同一区域，可能在白蛋白分子的一个共同腔内，但这样的腔足够大以容纳两种配体。
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