CALCIUM STOICHIOMETRY DETERMINATION FOR CALCIUM-BINDING PROTEINS BY ELECTROSPRAY-IONIZATION MASS-SPECTROMETRY
CALCIUM STOICHIOMETRY DETERMINATION FOR CALCIUM-BINDING PROTEINS BY ELECTROSPRAY-IONIZATION MASS-SPECTROMETRY
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DOI：
10.1021/ac00095a013
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发表时间：
1994-12-01
影响因子：
7.4
通讯作者：
LOO, JA
中科院分区：
文献类型：
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作者：
HU, PF;YE, QZ;LOO, JA
采用电喷雾电离质谱法测定钙结合蛋白的钙结合化学计量比。牛钙调素、牛α-乳清蛋白和兔小白蛋白分别与4、1和2个钙离子特异结合，这与以前报道的用其他物理方法获得的结果一致。这种质谱学方法也可以应用于与多种金属离子结合的蛋白质。测定了人基质分解蛋白催化区与锌离子和钙离子结合的化学计量比分别为3和2。
Electrospray ionization mass spectrometry was used for the determination of calcium-binding stoichiometry for calcium-binding proteins. Bovine calmodulin, bovine alpha-lactalbumin, and rabbit parvalbumin were found to bind specifically to 4, 1, and 2 Ca2+ ions, respectively, in agreement with previously reported results obtained by using other physical methods. This mass spectrometry method could also be applied to proteins that bind more than one type of metal ion. The Zn2+- and Ca2+-binding stoichiometries for human stromelysin catalytic domain were determined to be 3 and 2, respectively.