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Membrane association and some characteristics of the ethylene forming enzyme from etiolated pea seedlings
Year:
1982
Authors :
Achilea, Oded
;
.
Chalutz, Edo
;
.
Fuchs, Yoram
;
.
Volume :
105
Co-Authors:

Mattoo, A.K., Department of Plant Genetics, The Weizmann Institute of Science, Rehovot, Israel, Division of Fruit and Vegetable Storage, The Volcani Center, Bet-Dagan, Israel
Achilea, O., Division of Fruit and Vegetable Storage, The Volcani Center, Bet-Dagan, Israel
Fuchs, Y., Division of Fruit and Vegetable Storage, The Volcani Center, Bet-Dagan, Israel
Chalutz, E., Department of Plant Genetics, The Weizmann Institute of Science, Rehovot, Israel, Division of Fruit and Vegetable Storage, The Volcani Center, Bet-Dagan, Israel

Facilitators :
From page:
271
To page:
278
(
Total pages:
8
)
Abstract:
When freshly prepared homogenates of etiolated pea (Pisum sativum L. cv Calvedon) subhook segments were fractionated by high speed centrifugation, the enzyme catalyzing the conversion of 1-aminocyclopropane-l-carboxylic acid (ACC) to ethylene was found associated with the particulate fraction. However, on aging the homogenates at 5°C prior to fractionation, 50 to 75% of the enzyme activity partitioned into the soluble fraction; this solubilization led to a highly activated enzyme form. Both the particulate and soluble enzyme exhibited non-linear substrate saturation kinetics and were inhibited to similar extents by ascorbic acid, EDTA, CoCl2 and limiting oxygen. However, they differed in their response to incubation with n-propylgallate, dithiothreitol, CaCl2 and 100% oxygen. Calcium stimulated only the particulate form and increased both the 'low Km' for ACC from 2.99 to 5.58 mM and apparent Vmax from 88 to 285 nl/mg protein/h. © 1982 Academic Press, Inc.
Note:
Related Files :
article
cell membrane
ethylene forming enzyme
Kinetics
lyase
metabolism
plant
Plants
Support, U.S. Gov't, Non-P.H.S.
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Related Content
More details
DOI :
10.1016/S0006-291X(82)80041-7
Article number:
0
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
19869
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:32
You may also be interested in
Scientific Publication
Membrane association and some characteristics of the ethylene forming enzyme from etiolated pea seedlings
105

Mattoo, A.K., Department of Plant Genetics, The Weizmann Institute of Science, Rehovot, Israel, Division of Fruit and Vegetable Storage, The Volcani Center, Bet-Dagan, Israel
Achilea, O., Division of Fruit and Vegetable Storage, The Volcani Center, Bet-Dagan, Israel
Fuchs, Y., Division of Fruit and Vegetable Storage, The Volcani Center, Bet-Dagan, Israel
Chalutz, E., Department of Plant Genetics, The Weizmann Institute of Science, Rehovot, Israel, Division of Fruit and Vegetable Storage, The Volcani Center, Bet-Dagan, Israel

Membrane association and some characteristics of the ethylene forming enzyme from etiolated pea seedlings
When freshly prepared homogenates of etiolated pea (Pisum sativum L. cv Calvedon) subhook segments were fractionated by high speed centrifugation, the enzyme catalyzing the conversion of 1-aminocyclopropane-l-carboxylic acid (ACC) to ethylene was found associated with the particulate fraction. However, on aging the homogenates at 5°C prior to fractionation, 50 to 75% of the enzyme activity partitioned into the soluble fraction; this solubilization led to a highly activated enzyme form. Both the particulate and soluble enzyme exhibited non-linear substrate saturation kinetics and were inhibited to similar extents by ascorbic acid, EDTA, CoCl2 and limiting oxygen. However, they differed in their response to incubation with n-propylgallate, dithiothreitol, CaCl2 and 100% oxygen. Calcium stimulated only the particulate form and increased both the 'low Km' for ACC from 2.99 to 5.58 mM and apparent Vmax from 88 to 285 nl/mg protein/h. © 1982 Academic Press, Inc.
Scientific Publication
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