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פותח על ידי קלירמאש פתרונות בע"מ -
Phosphodiesterase activities in transgenic tobacco plants associated with the movement protein of tobacco mosaic virus
Year:
1992
Source of publication :
Theoretical and Applied Genetics
Authors :
פרל, מאיר
;
.
Volume :
84
Co-Authors:
Perl, M., Department of Biology, Washington University, Box 1137, St. Louis, 63130, MO, United States
Gafni, R., Department of Biology, Washington University, Box 1137, St. Louis, 63130, MO, United States
Beachy, R.N., Department of Biology, Washington University, Box 1137, St. Louis, 63130, MO, United States
Facilitators :
From page:
730
To page:
734
(
Total pages:
5
)
Abstract:
Hydrolytic activities of leaf extracts from normal and transgenic plants, with (+ MP) and without (-MP) the movement protein of tobacco mosaic virus, were examined. In the + MP transgenic plants, as compared with non-transgenic and - MP plants, higher hydrolytic activities were found on the following substrates: bis-(nitrophenyl)-phosphate (BPNPP, phosphodiesterase), p-nitrophenyl-(phenyl)-phosphate (PNPPP, nucleotidephosphodiesterase) and thymidine-3′-monophosphate p-nitrophenyl ester (T3MPP; 3′nucleotide phosphodiesterase.) The + MP plant lines, as compared with other transgenic plants, exhibited higher nucleotide-phosphodiesterase activity in the soluble as well as in the membrane fraction. Substrate concentration kinetic studies revealed the presence of a nucleotide-phospho-diesterase with a high substrate affinity in the +MP extracts in addition to the enzyme with a relatively low substrate affinity present also in the - MP transgenic plants. This "high affinity" enzyme could be removed from the soluble fraction by precipitation with anti-MP serum, indicating its possible association with the movement protein. © 1992 Springer-Verlag.
Note:
Related Files :
Movement protein
Phosphodiesterase
transgenic plants
עוד תגיות
תוכן קשור
More details
DOI :
10.1007/BF00224177
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
18453
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:21
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Scientific Publication
Phosphodiesterase activities in transgenic tobacco plants associated with the movement protein of tobacco mosaic virus
84
Perl, M., Department of Biology, Washington University, Box 1137, St. Louis, 63130, MO, United States
Gafni, R., Department of Biology, Washington University, Box 1137, St. Louis, 63130, MO, United States
Beachy, R.N., Department of Biology, Washington University, Box 1137, St. Louis, 63130, MO, United States
Phosphodiesterase activities in transgenic tobacco plants associated with the movement protein of tobacco mosaic virus
Hydrolytic activities of leaf extracts from normal and transgenic plants, with (+ MP) and without (-MP) the movement protein of tobacco mosaic virus, were examined. In the + MP transgenic plants, as compared with non-transgenic and - MP plants, higher hydrolytic activities were found on the following substrates: bis-(nitrophenyl)-phosphate (BPNPP, phosphodiesterase), p-nitrophenyl-(phenyl)-phosphate (PNPPP, nucleotidephosphodiesterase) and thymidine-3′-monophosphate p-nitrophenyl ester (T3MPP; 3′nucleotide phosphodiesterase.) The + MP plant lines, as compared with other transgenic plants, exhibited higher nucleotide-phosphodiesterase activity in the soluble as well as in the membrane fraction. Substrate concentration kinetic studies revealed the presence of a nucleotide-phospho-diesterase with a high substrate affinity in the +MP extracts in addition to the enzyme with a relatively low substrate affinity present also in the - MP transgenic plants. This "high affinity" enzyme could be removed from the soluble fraction by precipitation with anti-MP serum, indicating its possible association with the movement protein. © 1992 Springer-Verlag.
Scientific Publication
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