ISOLATION OF AN ACTOMYOSIN-LIKE PROTEIN COMPLEX FROM SLIME MOLD PLASMODIUM AND SEPARATION OF COMPLEX INTO ACTIN- AND MYOSIN-LIKE FRACTIONS

被引:94
作者
ADELMAN, MR
TAYLOR, EW
机构
[1] Department of Biophysics, University of Chicago, Chicago, Illinois
关键词
D O I
10.1021/bi00840a046
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
Extracts of the plasmodium of Physarum polycephalum prepared with various homogenization media contained a calcium-activated adenosine triphosphatase and a rapidly sedimenting actin-like protein. When plasmodial extracts prepared with 0.05 m sodium pyrophosphate-0.01 m Tris-maleate (pH 6.8) were fractionated by precipitation with ammonium sulfate, the adenosine triphosphatase and the rapidly sedimenting protein were isolated as a partially purifled actomyosin-like complex. As judged by viscometry, boundary and zone sedimentation, and electron microscopy slime mold actomyosin was basically similar to muscle actomyosin but differed in having a greater solubility at low ionic strength and a lower myosin:actin ratio. After desalting on Sephadex G-25, slime mold actomyosin was resolved into partially purified actin- and myosin-like components by gel chromatography on Sephadex G-200 at low ionic strength. © 1969, American Chemical Society. All rights reserved.
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页码:4964 / +
页数:1
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