Reaction of reduced disulfide bonds in α-lactalbumin and β-lactoglobulin with acrylonitrile
Reaction of reduced disulfide bonds in α-lactalbumin and β-lactoglobulin with acrylonitrile
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α-乳清蛋白和β-乳球蛋白中还原的二硫键与丙烯腈的反应
DOI：
10.1016/0003-9861(61)90178-3
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发表时间：
1961
影响因子：
3.9
通讯作者：
T. S. Seibles
中科院分区：
文献类型：
--
作者：
L. Weil;T. S. Seibles
α-乳清蛋白和β-乳球蛋白的二硫键与β-巯基乙醇的还原以及随后与丙烯腈的反应是特异的，并且根据蛋白质衍生物的总氨基酸分析，该反应仅限于硫醇基团。该反应导致半胱氨基残基的定量和特异性转化为S-氰乙基半胱氨酸基。酸解后，氰乙基半胱氨基被定量转化为S-羧乙基半胱氨酸，并进行了分析测定。
Reduction of disulfide bonds of α-lactalbumin and β-lactoglobulin with β-mercaptoethanol and subsequent reaction with acrylonitrile was shown to be specific and was confined to the thiol groups, as determined by total amino acid analysis of the protein derivatives. The reaction results in the quantitative and specific conversion of the cysteinyl residues toS-cyanoethylcysteinyl groups. Upon acid hydrolysis, theS-cyanoethylcysteinyl groups were converted quantitatively toS-carboxyethylcysteine and were determined analytically as such.