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Titolo:
BAFILOMYCIN A1 IS A NONCOMPETITIVE INHIBITOR OF THE TONOPLAST H-ATPASE OF MAIZE COLEOPTILES()
Autore:
WHITE PJ;
Indirizzi:
HORT RES INT,DEPT CELL PHYSIOL E MALLING ME19 6BJ KENT ENGLAND
Titolo Testata:
Journal of Experimental Botany
fascicolo: 279, volume: 45, anno: 1994,
pagine: 1397 - 1402
SICI:
0022-0957(1994)45:279<1397:BAIANI>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
VACUOLAR ATPASE; CORN COLEOPTILES; PROTON PUMP; PYROPHOSPHATASE; MEMBRANE; MICROORGANISMS; PURIFICATION; TRANSPORT; VESICLES; ROOTS;
Keywords:
BAFILOMYCIN A1; COLEOPTILE; H+-ATPASE (VACUOLAR); MAIZE; ZEA MAYS L;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
29
Recensione:
Indirizzi per estratti:
Citazione:
P.J. White, "BAFILOMYCIN A1 IS A NONCOMPETITIVE INHIBITOR OF THE TONOPLAST H-ATPASE OF MAIZE COLEOPTILES()", Journal of Experimental Botany, 45(279), 1994, pp. 1397-1402

Abstract

When microsomal membranes from maize (Zea mays L. cv. Clipper) coleoptiles were separated by isopycnic centrifugation on a continuous 10-45% sucrose gradient, bafilomycin A1-inhibited ATPase activity co-localized with the activities of the tonoplast marker-enzymes, nitrate-inhibited ATPase and K+-dependent pyrophosphatase. Thus, bafilomycin A1 is a specific inhibitor of the vacuolar H+-ATPase of maize coleoptiles. Inhibition of the vacuolar H+-ATPase by bafilomycin A1 was strictly dependent upon the concentration of the enzyme present in the assay medium, suggesting a stoichiometric association between bafilomycin A1 and the vacuolar H+-ATPase. In tonoplast-enriched preparations, half-maximal inhibition was obtained at 43 pmol bafilomycin A1 mg(-1) protein. Bafilomycin A1 inhibited the vacuolar H+-ATPase in a simple non-competitive manner: increasing bafilomycin A1 concentrations reduced the V-max of the Hf-ATPase, but had no effect on its K-m towards ATP.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 04:41:06