Dimeric structure of H+‐translocating pyrophosphatase from pumpkin vacuolar membranes

FEBS Letters

Ohsumi, Yoshinori¹  Sato, Masa H.³  Maeshima, Masayoshi²  Yoshida, Masasuke³ 

[1] Department of Biology, University of Tokyo, Komaba, Tokyo 153, Japan;Institute of Low Temperature Science, Hokkaido University, Sapporo 060, Japan;Department of Life Science, Tokyo Institute of Technology, Nagatsuta 4259, Yokohama 227, Japan

关键词: H+-translocating pyrophosphatase;    Plant vacuole;    Radiation inactivation;    Pumpkin;    Chaps;    3-[(3-cholamidepropyl)-dimethylammonio]-1-propanesulfonate;    DTT;    dithiothreitol;    PPase;    pyrophosphatase;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/0014-5793(91)81254-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Vacuolar membrane H⁺-translocating pyrophosphatase (H⁺-PPase) was purified from pumpkin seedlings. Its enzymatic properties including molecular size of constituting polypeptide (75 kDa) were very similar to those of mung bean H⁺-PPase [(1989) J. Biol. Chem. 264, 20068–20073]. The native, functional molecular size of the pumpkin H⁺-PPase was estimated to be 135–139 kDa from gel permeation HPLC of the purified enzyme in the presence of detergent and from radiation inactivation of the enzyme in vacuolar membranes. It is concluded that native, functional pumpkin H⁺-PPase, and also probably H⁺-PPases from other plants, is a dimer of 75 kDa subunits.

【 授权许可】

Unknown