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פותח על ידי קלירמאש פתרונות בע"מ -
Characterization of plasmalemma ATPase from apple fruit
Year:
1983
Source of publication :
Phytochemistry
Authors :
בן-אריה, רות
;
.
לוריא, סוזן
;
.
Volume :
22
Co-Authors:
Lurie, S., Division of Fruit and Vegetable Storage, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Ben-Arie, R., Division of Fruit and Vegetable Storage, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Facilitators :
From page:
49
To page:
52
(
Total pages:
4
)
Abstract:
The ATPase found in the 80000g pellet of apple fruit showed a pH optimum of 6, was inhibited by divalent cations and stimulated by monovalent cations. The enzyme was specific for ATP and inhibited by diethylstilbestrol and dicyclohexylcarbodiimide, while unaffected by oligomycin and the uncoupler SF 6874. The Km for ATP was 0.48 mM, Vmax1.2,μmol Pi/mg protein/min. Mg2+ was a competitive inhibitor to ATP; Ki0.7 mM. As the apple ripened from preclimacteric to postclimacteric, the ATPase activity increased more than two-fold. © 1983.
Note:
Related Files :
Apple
apple fruit
cation effects.
Malus sylvestris
plasmalemma ATPase
Rosaceae
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/S0031-9422(00)80056-4
Article number:
0
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
26622
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:24
Scientific Publication
Characterization of plasmalemma ATPase from apple fruit
22
Lurie, S., Division of Fruit and Vegetable Storage, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Ben-Arie, R., Division of Fruit and Vegetable Storage, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Characterization of plasmalemma ATPase from apple fruit
The ATPase found in the 80000g pellet of apple fruit showed a pH optimum of 6, was inhibited by divalent cations and stimulated by monovalent cations. The enzyme was specific for ATP and inhibited by diethylstilbestrol and dicyclohexylcarbodiimide, while unaffected by oligomycin and the uncoupler SF 6874. The Km for ATP was 0.48 mM, Vmax1.2,μmol Pi/mg protein/min. Mg2+ was a competitive inhibitor to ATP; Ki0.7 mM. As the apple ripened from preclimacteric to postclimacteric, the ATPase activity increased more than two-fold. © 1983.
Scientific Publication
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