Purified vacuolar inorganic pyrophosphatase consisting of a 75-kDa polypeptide can pump H+ into reconstituted proteoliposomes.
J Biol Chem
; 269(9): 6725-8, 1994 Mar 04.
Article
en En
| MEDLINE
| ID: mdl-8120031
ABSTRACT
Inorganic pyrophosphatase was purified to homogeneity from the vacuolar membranes of pumpkin hypocotyl tissue. The purified Inorganic pyrophosphatase consists of a single kind of 75-kDa polypeptide, and the stacked molecules with a repeating unit of 5.8 x 3.8 nm are seen under electron micrography. It exhibits H(+)-translocating activity across membranes coupled with PPi hydrolysis when it is reconstituted into proteoliposomes. A monovalent cation is required for the H+ translocation with the K+ ion being the most effective, but evidence for active transport of 42K+ into proteoliposomes was not obtained under the conditions tested. The hydrolysis of PPi by the reconstituted proteoliposomes is stimulated by the addition of a H+ ionophore, carbonyl cyanide p-trifluoromethyoxyphenylhydrazone, but not by a K+ ionophore, valinomycin. Both hydrolysis of PPi and PPi-dependent H+ translocation of the proteoliposomes are inhibited by N,N'-dicyclohexylcarbodiimide.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteolípidos
/
Pirofosfatasas
/
Vacuolas
/
Verduras
Idioma:
En
Revista:
J Biol Chem
Año:
1994
Tipo del documento:
Article
País de afiliación:
Japón