נגישות
menu      
Advanced Search
Syntax
Search...
Volcani treasures
About
Terms of use
Manage
Community:
אסיף מאגר המחקר החקלאי
Powered by ClearMash Solutions Ltd -
Influence of Ethylene on S-adenosylmethionine Decarboxylase Activity in Etiolated Pea Seedlings
Year:
1985
Source of publication :
Journal of Plant Physiology
Authors :
Apelbaum, Akiva
;
.
Goldlust, Arie
;
.
Icekson, Isaac
;
.
Volume :
119
Co-Authors:
Icekson, I., Dept. of Fruit and Vegetable Storage, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Goldlust, A., Dept. of Fruit and Vegetable Storage, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Apelbaum, A., Dept. of Fruit and Vegetable Storage, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Facilitators :
From page:
335
To page:
345
(
Total pages:
11
)
Abstract:
S-adenosyl-L-methionine decarboxylase was detected in crude extract from the plumular hook of etiolated pea seedlings. The enzyme showed a Km of 0.2mM for S-adenosyl-Lmethionine and a Vmax of 4.76 nmol/mg protein/h. It was not activated by putrescine or by Mg++ and was inhibited by methyl glyoxal-bis-guanyl hydrazone with an I50 of 1µM. Treatment of pea seedlings with ethylene resulted in a 75 % reduction of the enzyme activity with an I50 of 0.3 µl/1 and a maximal effect at 6µl/l. The reduction was observed within 1 hour after exposure to ethylene, reaching a maximum at 18 hours. Upon transferring the ethylenetreated plants to an ethylene-free atmosphere the enzyme gradually recovered from the inhibition, showing a complete recovery within 6 hours. Exposing pea seedlings to treatments that caused a reduction in the endogenous level of ethylene resulted in a 30–48 % increase in the enzyme activity. In view of the results of this study, the possibility that ethylene at the endogenous level might regulate S-adenosyl-L-methionine decarboxylase activity is discussed. © 1985, Gustav Fischer Verlag, Stuttgart. All rights reserved.
Note:
Related Files :
1-aminocyclopropane-l-carboxylic acid
ACC
arginine decarboxylase
AVG
ethylene
MGBG
Pisum sativum
Show More
Related Content
More details
DOI :
10.1016/S0176-1617(85)80101-2
Article number:
0
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
27362
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:30
Scientific Publication
Influence of Ethylene on S-adenosylmethionine Decarboxylase Activity in Etiolated Pea Seedlings
119
Icekson, I., Dept. of Fruit and Vegetable Storage, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Goldlust, A., Dept. of Fruit and Vegetable Storage, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Apelbaum, A., Dept. of Fruit and Vegetable Storage, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Influence of Ethylene on S-adenosylmethionine Decarboxylase Activity in Etiolated Pea Seedlings
S-adenosyl-L-methionine decarboxylase was detected in crude extract from the plumular hook of etiolated pea seedlings. The enzyme showed a Km of 0.2mM for S-adenosyl-Lmethionine and a Vmax of 4.76 nmol/mg protein/h. It was not activated by putrescine or by Mg++ and was inhibited by methyl glyoxal-bis-guanyl hydrazone with an I50 of 1µM. Treatment of pea seedlings with ethylene resulted in a 75 % reduction of the enzyme activity with an I50 of 0.3 µl/1 and a maximal effect at 6µl/l. The reduction was observed within 1 hour after exposure to ethylene, reaching a maximum at 18 hours. Upon transferring the ethylenetreated plants to an ethylene-free atmosphere the enzyme gradually recovered from the inhibition, showing a complete recovery within 6 hours. Exposing pea seedlings to treatments that caused a reduction in the endogenous level of ethylene resulted in a 30–48 % increase in the enzyme activity. In view of the results of this study, the possibility that ethylene at the endogenous level might regulate S-adenosyl-L-methionine decarboxylase activity is discussed. © 1985, Gustav Fischer Verlag, Stuttgart. All rights reserved.
Scientific Publication
You may also be interested in