STUDIES ON INTERACTION OF MAGNESIUM, CALCIUM AND STRONTIUM IONS WITH NATIVE AND CHEMICALLY MODIFIED HUMAN SERUM ALBUMIN
STUDIES ON INTERACTION OF MAGNESIUM, CALCIUM AND STRONTIUM IONS WITH NATIVE AND CHEMICALLY MODIFIED HUMAN SERUM ALBUMIN
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DOI：
10.1042/bj0840152
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发表时间：
1962-01-01
影响因子：
4.1
通讯作者：
PERKINS, DJ
中科院分区：
文献类型：
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作者：
IRONS, LI;PERKINS, DJ
Ca2+、Mg2+ 和 Sr2+ 离子与天然和化学修饰的人白蛋白的相互作用相似。对天然白蛋白的相对结合亲和力为：Ca2+ > Mg2+ > Sr2+ 离子，对修饰白蛋白的相对结合亲和力为Ca2+ > Mg2+、Sr2+ 离子。与天然、酯化和乙酰化白蛋白的结合主要通过对非特异性位点的静电吸引来控制，尽管也发现了与天然白蛋白特异性位点的结合。通过特定位点与磷酸化和溴乙酰化白蛋白结合。在存在柠檬酸根离子的情况下，Ca2+ 离子在 pH 值低于 5. 2 时作为带负电荷的柠檬酸钙复合物与天然白蛋白结合，在 pH 值高于 5. 2 时作为游离离子结合。
Interactions of Ca2+, Mg2+ and Sr2+ ions with native and chemically modified human albumin are similar. The relative binding affinity to native albumin is: Ca2+ > Mg2+ > Sr2+ ions, and to the modified albumin Ca2+> Mg2+, Sr2+ ions. The binding to native, esterified and acetylated albumins is governed mainly by electrostatic attraction to non-specific sites, although with native albumin specific site binding has also been found. Binding to phosphorylated and bromoacetylated albumins occurs through specific sites. In the presence of citrate ions, Ca2+ ions are bound to native albumin at pH values below 5. 2 as a negatively charged calcium citrate complex and at pH values above 5 2 as the free ion.