SYNEXIN PROTEIN IS NON-SELECTIVE IN ITS ABILITY TO INCREASE CA-2+-DEPENDENT AGGREGATION OF BIOLOGICAL AND ARTIFICIAL MEMBRANES

被引:20
作者
MORRIS, SJ
HUGHES, JMX
机构
[1] Department of Neurochemistry Max Planck Institute for Biophysical Chemistry
关键词
D O I
10.1016/0006-291X(79)90624-7
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
Synexin, a soluble protein which increases the specificity of Ca2+ to aggregate isolated bovine chromaffin granules was prepared from bovine adrenal medullary tissue by the method of Creutz, Pazoles and Pollard (J. Biol. Chem. 253, 2858-2866, 1978). We also find that synexin increases both the initial rate and final amplitude of Ca2+-promoted aggregation of granule membranes. This effect is Ca2+-specific. However in contrast to Creutz et al, we find that synexin also potentiates aggregation of adrenal medulla and liver mitochondria and microsomes as well as phosphatidylserine vesicles. This lack of membrane specificity argues against the suggestion of Creutz et al that synexin specifically binds the granule to the plasma membrane prior to exocytosis in vivo. © 1979.
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页码:345 / 350
页数:6
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