Investigation of calcium-induced, noncovalent association of calmodulin with melittin by electrospray ionization mass spectrometry

被引：63

作者：

Nemirovskiy, OV ^{[1
]}

Ramanathan, R ^{[1
]}

Gross, ML ^{[1
]}

机构：

[1] WASHINGTON UNIV,DEPT CHEM,ST LOUIS,MO 63130

来源：

JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY | 1997年 / 8卷 / 08期

关键词：

D O I：

10.1016/S1044-0305(97)00086-X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Noncovalent association of Ca2+-loaded calmodulin with a target peptide melittin was studied by electrospray ionization mass spectrometry (ESI-MS). ESI-MS does not reveal any binding of the apocalmodulin to the melittin. Partial loading of calmodulin with calcium leads to weak association with melittin. Upon binding of two calcium ions to the protein, changes in the conformation of calmodulin occur; these changes are sufficient to promote binding of melittin. Saturation of the protein with Ca2+ (a distribution of up to seven calcium ions is detected) induces a large increase of the binding to melittin. The stoichiometry of peptide binding to calmodulin is 1:1. (C) 1997 American Society for Mass Spectrometry.

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页码：809 / 812

页数：4

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