Document Detail

Phosphodiesterase activities in transgenic tobacco plants associated with the movement protein of tobacco mosaic virus.
MedLine Citation:
PMID:  24201366     Owner:  NLM     Status:  In-Data-Review    
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.
M Perl; R Gafni; R N Beachy
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik     Volume:  84     ISSN:  0040-5752     ISO Abbreviation:  Theor. Appl. Genet.     Publication Date:  1992 Aug 
Date Detail:
Created Date:  2013-11-08     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0145600     Medline TA:  Theor Appl Genet     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  730-4     Citation Subset:  -    
Department of Biology, Washington University, Box 1137, 63130, St. Louis, MO, USA.
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