TERBIUM REPLACEMENT OF CALCIUM IN PARVALBUMIN

被引：64

作者：

SOWADSKI, J ^{[1
]}

CORNICK, G ^{[1
]}

KRETSINGER, RH ^{[1
]}

机构：

[1] UNIV VIRGINIA,DEPT BIOL,CHARLOTTESVILLE,VA 22901

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1978年 / 124卷 / 01期

关键词：

D O I：

10.1016/0022-2836(78)90151-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Carp muscle calcium binding parvalbumin, crystallized in 2.9 m-ammonium sulfate, can bind two Tb3+ ions, which displace the two Ca2+ ions normally present. The Ca2+ co-ordinated in the loop between the E and the F α-helices is displaced at low Tb3+ concentrations; whereas the Ca2+ at the CD site is replaced only at higher Tb3+ concentration. There is not a third Tb3+ site as had been suggested in interpretations of Tb3+ fluorescence experiments performed without ammonium sulfate. A third electron density peak in the difference Fourier maps is tentatively assigned to a sulfate ion co-ordinating the EF site Tb3+ ion. © 1978.

引用

页码：123 / 132

页数：10

共 17 条

[1] BINDING OF CALCIUM TO MUSCULAR PARVALBUMINS [J].