PURIFICATION AND IMMUNOLOGICAL COMPARISON OF THE TONOPLAST H+-PYROPHOSPHATASE FROM CELLS OF CATHARANTHUS-ROSEUS AND LEAVES FROM MESEMBRYANTHEMUM-CRYSTALLINUM PERFORMING C-3-PHOTOSYNTHESIS AND THE OBLIGATE CAM-PLANT KALANCHOE-DAIGREMONTIANA

被引：10

作者：

BECKER, A

CANUT, H

LUTTGE, U

MAESHIMA, M

MARIGO, G

RATAJCZAK, R

机构：

[1] UNIV TOULOUSE 3,CTR PHYSIOL VEGETALE,CNRS,URA 1457,F-31062 TOULOUSE,FRANCE

[2] NAGOYA UNIV,SCH AGR SCI,BIOCHEM LAB,NAGOYA,AICHI 46401,JAPAN

[3] UNIV GRENOBLE 1,BIOL ALPINE LAB,F-38041 GRENOBLE,FRANCE

来源：

JOURNAL OF PLANT PHYSIOLOGY | 1995年 / 146卷 / 1-2期

关键词：

H+-PYROPHOSPHATASE (H+-PP(I)ASE); CRASSULACEAN-ACID METABOLISM; KALANCHOE DAIGREMONTIANA; CATHARANTHUS ROSEUS; MESEMBRYANTHEMUM CRYSTALLINUM;

D O I：

10.1016/S0176-1617(11)81972-3

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

The tonoplast H+-pyrophosphatase (EC 3.6.1.1) from photosynthetically inactive cell cultures of the C-3-plant Catharanthus roseus (L.) G. Don., and from leaves of the C-3/CAM-intermediate plant Mesembryanthemum crystallinum L. in the C-3-state and of the obligate CAM-plant Kalanchoe daigremontiana Hamet et Perrier de la Bathie, was purified using Mono Q anion-exchange and Superose 6 size-exclusion fast protein liquid chromatography. The combination of both chromatographical techniques led to a single polypeptide with an apparent molecular mass of 72 kDa exhibiting K+-stimulated pyrophosphate hydrolysis activity in preparations from C. roseus and M. crystallinum and to two polypeptides (72 and 70 kDa) in hydrolytic active fractions from K. daigremontiana. These polypeptides cross-reacted with an antiserum against the tonoplast inorganic H+-pyrophosphatase of Vigna radiata L. cv. Wilczek. The possible identity of the 70 kDa polypeptide of K. daigremontiana is discussed.

引用

页码：88 / 94

页数：7

共 31 条

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