A pmr study of the effects of pH and anion and metal ion binding of the histidyl residues of ovotransferrin.
A pmr study of the effects of pH and anion and metal ion binding of the histidyl residues of ovotransferrin.
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PMR 研究 pH 值以及阴离子和金属离子对卵转铁蛋白组氨酰残基结合的影响。
DOI：
10.1016/s0162-0134(00)80131-2
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发表时间：
1981
影响因子：
3.9
通讯作者：
Woodworth,RC
中科院分区：
文献类型：
--
作者：
Alsaadi,BM;Williams,RJ;Woodworth,RC
卵转铁蛋白的高分辨率质子磁共振研究表明，四组C（2）-H组氨酰共振的主要芳香包膜的低场清晰的分辨率。滴定的蛋白质的协同阴离子，草酸，丙二酸，和2，6-吡啶二甲酸，和阴离子加金属离子的存在和不存在下，揭示了6个组氨酸参与的结合位点。这些组氨酸，每个结合位点有三个，彼此靠近。在每个结合位点中，一个组氨酸参与与阴离子的结合，两个组氨酸参与与金属离子的结合。
High resolution proton magnetic resonance studies of ovotransferrin show clear resolution of four groups of C(2)-H histidyl resonances to low field of the major aromatic envelope. Titrations of the protein in the absence and presence of synergistic anions, oxalic acid, malonic acid, and 2,6-dipicolinic acid, and anions plus metal ions reveal that six histidines are involved in the binding sites. These histidines, three in each binding site, are near to one another. In each binding site one histidine is involved in binding to anions and two are involved in binding to metal ions.