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Salt‐induced cooperativity in ATPase activity of plasma membrane‐enriched fractions from cultured Citrus cells: kinetic evidence
Year:
1990
Source of publication :
Physiologia Plantarum
Authors :
Ben Hayyim, Gosal
;
.
Ran, Uri
;
.
Volume :
80
Co-Authors:
Ben‐Hayyim, G., Inst. of Horticulture, Aro, Volcani Center, P.O.Box 6, Bet Dagan, 50250, Israel
Ran, U., Inst. of Horticulture, Aro, Volcani Center, P.O.Box 6, Bet Dagan, 50250, Israel
Facilitators :
From page:
210
To page:
216
(
Total pages:
7
)
Abstract:
ATPase activity was studied in plasma membrane‐enriched fractions prepared from cultured Citrus sinensis L. cv. Osbeck cells. In general, properties of the plasma membrane ATPase from cultured cells, such as optimal pH and temperature. Vmax and Km were similar to those already observed in higher plants. The effects of high salt concentrations on ATPase activity were studied in membrane fractions derived from salt‐sensitive and salt‐tolerant cells grown in the presence or absence of salt. NaCl did not have an in vivo effect on Vmax and the apparent Km value for ATP. However, high concentrations of NaCl, or KCl, added in vitro, induced cooperativity in the enzyme and reduced the affinity of the enzyme for its substrate. Isoosmolar concentrations of sucrose or choline chloride failed to do so. Our results suggest that the plasma membrane ATPase of Citrus cells has more than one substrate‐binding site on the native form of the enzyme which interact in the presence of salt and act independently in its absence. Copyright © 1990, Wiley Blackwell. All rights reserved
Note:
Related Files :
ATPase
Citrus cells
enzyme cooperativity
kinetic parameters
plasma membrane vesicles
salt
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Related Content
More details
DOI :
10.1111/j.1399-3054.1990.tb04398.x
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
31442
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 01:02
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Scientific Publication
Salt‐induced cooperativity in ATPase activity of plasma membrane‐enriched fractions from cultured Citrus cells: kinetic evidence
80
Ben‐Hayyim, G., Inst. of Horticulture, Aro, Volcani Center, P.O.Box 6, Bet Dagan, 50250, Israel
Ran, U., Inst. of Horticulture, Aro, Volcani Center, P.O.Box 6, Bet Dagan, 50250, Israel
Salt‐induced cooperativity in ATPase activity of plasma membrane‐enriched fractions from cultured Citrus cells: kinetic evidence
ATPase activity was studied in plasma membrane‐enriched fractions prepared from cultured Citrus sinensis L. cv. Osbeck cells. In general, properties of the plasma membrane ATPase from cultured cells, such as optimal pH and temperature. Vmax and Km were similar to those already observed in higher plants. The effects of high salt concentrations on ATPase activity were studied in membrane fractions derived from salt‐sensitive and salt‐tolerant cells grown in the presence or absence of salt. NaCl did not have an in vivo effect on Vmax and the apparent Km value for ATP. However, high concentrations of NaCl, or KCl, added in vitro, induced cooperativity in the enzyme and reduced the affinity of the enzyme for its substrate. Isoosmolar concentrations of sucrose or choline chloride failed to do so. Our results suggest that the plasma membrane ATPase of Citrus cells has more than one substrate‐binding site on the native form of the enzyme which interact in the presence of salt and act independently in its absence. Copyright © 1990, Wiley Blackwell. All rights reserved
Scientific Publication
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