通过钙调蛋白 - 琼脂糖亲和层析法从萝卜幼苗中纯化质膜钙ATP酶
Purification of the Plasma Membrane Ca2+-ATPase from Radish Seedlings by Calmodulin-Agarose Affinity Chromatography.
作者信息
Bonza C, Carnelli A, Rasi-Caldogno F
机构信息
Dipartimento di Biologia L. Gorini, Università di Milano, via G. Celoria 26, 20133 Milano, Italy (C.B., A.C., F.R.-C.)
出版信息
Plant Physiol. 1998 Feb 1;116(2):845-51. doi: 10.1104/pp.116.2.845.
Abstract
The Ca2+-ATPase of the plasma membrane (PM) of germinating radish (Raphanus sativus L.) seeds was purified by calmodulin (CaM)-affinity chromatography using a batch procedure. PM purified by aqueous two-phase partitioning was solubilized with n-dodecyl beta-d-maltoside and applied to a CaM-agarose matrix. After various washings with decreasing Ca2+ concentrations, the Ca2+-ATPase was eluted with 5 mm ethylenediaminetetraacetate (EDTA). The EDTA-eluted fraction contained about 25% of the loaded Ca2+-ATPase activity, with a specific activity 70-fold higher than that of the starting PM fraction. The EDTA-eluted fraction was highly enriched in a 133-kD polypeptide, which was identified as the PM Ca2+-ATPase by 125I-CaM overlay and fluorescein-isothiocyanate labeling. The PM Ca2+-ATPase cross-reacted with an antiserum against a putative Ca2+-ATPase of the Arabidopsis thaliana chloroplast envelope.
摘要
采用批量法，通过钙调蛋白（CaM）亲和层析对萌发萝卜（Raphanus sativus L.）种子质膜（PM）的Ca2 + -ATP酶进行了纯化。用正十二烷基β-D-麦芽糖苷溶解经双水相分配纯化的质膜，并将其应用于CaM-琼脂糖基质。在用浓度逐渐降低的Ca2 +进行各种洗涤后，用5 mM乙二胺四乙酸（EDTA）洗脱Ca2 + -ATP酶。经EDTA洗脱的部分含有约25%的加载Ca2 + -ATP酶活性，比起始质膜部分的比活性高70倍。经EDTA洗脱的部分高度富集一种133-kD多肽，通过125I-CaM覆盖和异硫氰酸荧光素标记鉴定为质膜Ca2 + -ATP酶。质膜Ca2 + -ATP酶与抗拟南芥叶绿体被膜假定Ca2 + -ATP酶的抗血清发生交叉反应。
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