DETERMINING CALCIUM-BINDING STOICHIOMETRY AND COOPERATIVITY OF PARVALBUMIN AND CALMODULIN BY MASS-SPECTROMETRY

被引：50

作者：

HU, PF ^{[1
]}

LOO, JA ^{[1
]}

机构：

[1] WARNER LAMBERT PARKE DAVIS, PARKE DAVIS PHARMACEUT RES, ANN ARBOR, MI 48105 USA

来源：

JOURNAL OF MASS SPECTROMETRY | 1995年 / 30卷 / 08期

关键词：

D O I：

10.1002/jms.1190300803

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The calcium-binding properties of parvalbumin and calmodulin were investigated by electrospray ionization mass spectrometry (ESI-MS). The two calcium sites of parvalbumin were found to be strongly cooperative in binding Ca2+ ion. Up to four calcium ions were found to bind to calmodulin at high calcium concentration levels. Strong cooperativity was detected between the third and fourth Ca2+ binding sites of calmodulin (ordered by loading sequence). Strong interactions were also indicated between the two halves of the calmodulin molecule. Demetallation of the gas-phase ions can occur during the desolvation process, especially for ESI of aqueous solutions. However, the ESI-MS methodology has the potential to provide insight into the intricate processes involved in metal site communications for other metalloproteins.

引用

页码：1076 / 1082

页数：7

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