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Phosphatase and ATPase activities in isonuclear lines of cytoplasmic male-sterile and male-fertile petunia
Year:
1993
Source of publication :
Theoretical and Applied Genetics
Authors :
Izhar, Shamay
;
.
Perl, Meir
;
.
Swartzberg, Dvora
;
.
Volume :
86
Co-Authors:
Perl, M., Department of Plant Genetics, ARO, The Volcani Center, Bet-Dagan, 50 250, Israel
Swartzberg, D., Department of Plant Genetics, ARO, The Volcani Center, Bet-Dagan, 50 250, Israel
Izhar, S., Department of Plant Genetics, ARO, The Volcani Center, Bet-Dagan, 50 250, Israel
Facilitators :
From page:
49
To page:
53
(
Total pages:
5
)
Abstract:
Soluble and membrane-bound fractions of plant leaves, cell suspension cultures and seedlings of petunia were examined for phosphohydrolase activity on p-nitrophenyl phosphate (pNPPase) and adenosine triphosphate (ATPase). One cytoplasmic male-sterile (CMS) and one fertile (F) line was examined for each tissue. Both pNPPase and ATPase exhibited a broad optimal activity between pH 5.5-7.0 for the membrane-bound fraction and between 4.5-7.0 for the soluble fractions. The activity of both were inhibited by divalent ions including Mg2+. At pH 7.2, the activities on various triphosphonucleotides were similar and they were hydrolyzed by a rate of 20-50% of that of ATP. Significant differences between CMS and F extracts were: (a) higher activities in CMS membranes; (b) lower Ea (energy of activation) values for activities in CMS membrane functions; (c) seedling and cell-culture CMS extracts exhibited a higher sensitivity to high temperature denaturation; (d) the hydrolase activity on monoand triphospho-cytosine compounds was significantly higher in CMS than in F membranes. © 1993 Springer-Verlag.
Note:
Related Files :
ATPase
Cytoplasmic male sterility
Petunia
Phosphatase
Show More
Related Content
More details
DOI :
10.1007/BF00223807
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
22412
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:51
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Scientific Publication
Phosphatase and ATPase activities in isonuclear lines of cytoplasmic male-sterile and male-fertile petunia
86
Perl, M., Department of Plant Genetics, ARO, The Volcani Center, Bet-Dagan, 50 250, Israel
Swartzberg, D., Department of Plant Genetics, ARO, The Volcani Center, Bet-Dagan, 50 250, Israel
Izhar, S., Department of Plant Genetics, ARO, The Volcani Center, Bet-Dagan, 50 250, Israel
Phosphatase and ATPase activities in isonuclear lines of cytoplasmic male-sterile and male-fertile petunia
Soluble and membrane-bound fractions of plant leaves, cell suspension cultures and seedlings of petunia were examined for phosphohydrolase activity on p-nitrophenyl phosphate (pNPPase) and adenosine triphosphate (ATPase). One cytoplasmic male-sterile (CMS) and one fertile (F) line was examined for each tissue. Both pNPPase and ATPase exhibited a broad optimal activity between pH 5.5-7.0 for the membrane-bound fraction and between 4.5-7.0 for the soluble fractions. The activity of both were inhibited by divalent ions including Mg2+. At pH 7.2, the activities on various triphosphonucleotides were similar and they were hydrolyzed by a rate of 20-50% of that of ATP. Significant differences between CMS and F extracts were: (a) higher activities in CMS membranes; (b) lower Ea (energy of activation) values for activities in CMS membrane functions; (c) seedling and cell-culture CMS extracts exhibited a higher sensitivity to high temperature denaturation; (d) the hydrolase activity on monoand triphospho-cytosine compounds was significantly higher in CMS than in F membranes. © 1993 Springer-Verlag.
Scientific Publication
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