钙调蛋白是四膜虫排出的刺丝泡的主要成分。
Calmodulin is a major component of extruded trichocysts from Paramecium tetraurelia.
作者信息
Rauh J J, Nelson D L
出版信息
J Cell Biol. 1981 Dec;91(3 Pt 1):860-5. doi: 10.1083/jcb.91.3.860.
Abstract
Extruded trichocysts are composed of a family of proteins with molecular weights between 15,000 and 20,000. We have used heat treatment and affinity chromatography on fluphenazine-Sepharose to purify calmodulinlike proteins from whole cells and from extruded trichocysts. The purified protein from trichocysts is indistinguishable from that of whole cells; it is heat-stable, activates brain phosphodiesterase in a Ca++-dependent fashion, changes mobility on SDS polyacrylamide gels in the presence of Ca++, contains 1 mol of trimethyllysine/17 kdaltons, and has the amino acid composition characteristic of calmodulins. Calmodulin is a major component of purified, extruded trichocysts, of which it represents between 1 and 10% by mass. The other proteins of the trichocyst also resemble calmodulin in several properties. Possible roles for calmodulin in the Ca++-activated extrusion of trichocysts is discussed.
摘要
射出刺丝囊由分子量在15,000至20,000之间的一族蛋白质组成。我们利用热处理以及在氟奋乃静-琼脂糖上进行亲和层析，从全细胞和射出刺丝囊中纯化类钙调蛋白。从刺丝囊中纯化得到的蛋白质与全细胞的蛋白质无法区分；它对热稳定，以Ca++依赖的方式激活脑磷酸二酯酶，在Ca++存在的情况下在SDS聚丙烯酰胺凝胶上改变迁移率，每17千道尔顿含有1摩尔三甲基赖氨酸，并且具有钙调蛋白的氨基酸组成特征。钙调蛋白是纯化的射出刺丝囊的主要成分，按质量计占1%至10%。刺丝囊的其他蛋白质在若干特性上也与钙调蛋白相似。文中讨论了钙调蛋白在Ca++激活的刺丝囊射出过程中的可能作用。
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本文引用的文献
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