Characterization of an Isolate of Cucumber mosaic cucumovirus from Radish (Raphanus sativus) in Iraq

2013 ◽  
Vol 12 (2) ◽  
pp. 115-119 ◽  
Author(s):  
Mustafa A. Adhab ◽  
Rakib A. Al-Ani
Keyword(s):  
Raphanus Sativus ◽  
Cucumber Mosaic Cucumovirus

scholarly journals Characterization of a Severe Strain of Cucumber Mosaic Cucumovirus Seedborne in Cowpea

Plant Disease ◽  
1998 ◽  
Vol 82 (4) ◽  
pp. 419-422 ◽  
Author(s):  
A. G. Gillaspie ◽  
M. R. Hajimorad ◽  
S. A. Ghabrial
Keyword(s):  
Nucleic Acid ◽  
Nucleic Acid Hybridization ◽  
Satellite Rna ◽  
Severe Strain ◽  
Cucumber Mosaic Cucumovirus ◽  
Hybridization Assays

A new seedborne strain of cucumber mosaic cucumovirus (CMV) that induces severe symptoms on many cowpea genotypes was detected in Georgia in 1994. This strain, designated CMV-Csb, is asymptomatic on tobacco, but it produces more severe cowpea stunt symptoms when present in combination with blackeye cowpea mosaic potyvirus than do the more prevalent CMV isolates. The new strain is seedborne in cowpea (1.5 to 37%), has no associated satellite RNA, and is classified as a member of subgroup I of CMV strains based on nucleic acid hybridization assays.

scholarly journals Characterization of Radish (Raphanus sativus) Storage Proteins

1984 ◽  
Vol 74 (3) ◽  
pp. 487-493 ◽  
Author(s):  
Monique Laroche ◽  
Lorette Aspart ◽  
Michel Delseny ◽  
Paul Penon
Keyword(s):  
Raphanus Sativus ◽  
Storage Proteins

Sinapine Esterase I. Characterization of Sinapine Esterase from Cotyledons of Raphanus sativus

1979 ◽  
Vol 34 (9-10) ◽  
pp. 715-720 ◽  
Author(s):  
Gerhild Nurmann ◽  
Dieter Strack
Keyword(s):  
Enzyme Activity ◽  
Esterase Activity ◽  
Raphanus Sativus ◽  
Sinapic Acid ◽  
Inhibitory Effect ◽  
Ph Optimum ◽  
Diisopropyl Fluorophosphate ◽  
E 600 ◽  
Red Radish

Abstract From cotyledons of Raphanus sativus (red radish) an esterase activity which catalyzes the hy­drolysis of sinapine into sinapic acid and choline has been isolated. The enzyme, which has a near absolute specificity, is not analogous with any esterase described in the literature. The reaction has a pH optimum of 8.5 and the apparent Km is 1.95 × 10-5 m. The enzyme is relatively insensi­tive to both physostigmine (eserine) {Ki = 1.73 × 10-4 m) and neostigmine (Ki = 2 .1 3 × 10-4 ᴍ). Diisopropyl fluorophosphate (DFP) showed no inhibition and diethyl p-nitrophenylphosphate (E 600) only a slight inhibitory effect at 10-5 ᴍ, respectively. Choline (10-2 ᴍ) was inhibitory but acetylcholine (10-2 ᴍ) stimulated the enzyme activity.

scholarly journals Biochemical characterization of Burkina red radish (Raphanus sativus) peroxidase

2018 ◽  
Vol 125 (1) ◽  
pp. 12518
Author(s):  
Mamounata Diao ◽  
Crépin I. Dibala ◽  
Brice N’cho Ayékoué ◽  
Mamoudou H. Dicko
Keyword(s):  
Raphanus Sativus ◽  
Biochemical Characterization ◽  
Red Radish
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