ISOLATION AND ELECTROPHORETIC PROPERTIES OF A CALCIUM-BINDING PROTEIN FROM THE CILIATE TETRAHYMENA-PYRIFORMIS

被引:41
作者
SUZUKI, Y [1 ]
HIRABAYASHI, T [1 ]
WATANABE, Y [1 ]
机构
[1] UNIV TSUKUBA, INST BIOL SCI, NIIHARI, IBARAKI 30031, JAPAN
关键词
D O I
10.1016/0006-291X(79)91618-8
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
A calcium-binding protein (TCBP) was isolated from the ciliate Tetrahymena pyriformis by a procedure which included 8 M urea extraction of the cell homogenate or boiling water extraction of acetone-dried powder of the cell, ammonium sulfate precipitation (60-80% saturation) and preparative electrophoresis on alkaline polyacrylamide gel. The TCBP has a molecular weight of 14,000 daltons and an isoelectric point of pH 4.0 and is easily detected in crude cell extracts by the change of electrophoretic mobility depending on Ca ion concentration. By equilibrium dialysis TCBP was found to bind to 2 moles of calcium per mole of the protein at a free calcium concentration of 10-4 M. On alkaline polyacrylamide gel, the TCBP interacts with rabbit skeletal muscle troponin I and with some material(s) of Tetrahymena origin to form Ca2+-dependent complexes. © 1979.
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页码:253 / 260
页数:8
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