scholarly journals Analysis of Several Popular Cultivars of Madagascar Periwinkle (Catharanthus roseus (L.) G. Don.) using Biochemical Markers

2013 ◽  
Vol 5 (4) ◽  
pp. 458-461
Author(s):  
Owk ANIEL KUMAR ◽  
Sape S. TATA ◽  
Kancharla PAVAN KUMAR

Band designs of esterase (EST), peroxidase (PO) and polyphenol oxidase (PPO) isozymes in several selected cultivars of Catharanthus roseus by using native polyacrylamide gel electrophoresis (PAGE) were investigated in this study. It was confirmed that cultivar differences in isozyme polymorphism can be revealed by applied electrophoretic patterns. Three isozyme systems produced a total of 16 bands with polymorphism ranged from 66.6-100%. Considering the patterns of isozyme variations in the five cultivars of Catharanthus roseus, it is evident that the cultivar ‘First kiss coral’ displayed crimson red petal with large white eye’ displayed demarked profiles of EST, PO and PPO isozymes than other cultivars. This is the first report on isozyme polymorphism in members of the Cathanarathus roseus (L.) G. Don.

1987 ◽  
Vol 67 (3) ◽  
pp. 713-717 ◽  
Author(s):  
A. HUSSAIN ◽  
W. BUSHUK ◽  
H. RAMIREZ ◽  
W. ROCA

An electrophoretic procedure was developed for discriminating cultivars of Desmodium ovalifolium on the basis of patterns of partially purified seed proteins. Electrophoresis was done on uniform 15% polycrylamide gels in basic (8.9) pH. The method produced satisfactory discrimination of eight cultivars used in its initial evaluation.Key words: Forage legume, Desmodium ovalifolium Guill et Perr., cultivar identification, polyacrylamide gel electrophoresis


1970 ◽  
Vol 118 (2) ◽  
pp. 303-310 ◽  
Author(s):  
H. Winkler ◽  
Heide Hörtnagl ◽  
H. Hörtnagl ◽  
A. D. Smith

Washed membranes of bovine adrenal chromaffin granules contained most of the cholesterol and phospholipids of the particle and 22% of the total protein. The protein/lipid ratio was about 0.45 (w/w). Dopamine(3,4-dihydroxyphenethylamine)β-hydroxylase, Mg2+-activated nucleoside triphosphatase and cytochrome b-559 activities were present in the membrane. ATP was the best substrate for the nucleoside triphosphatase, whose pH optimum was 6.4, Km 7×10−4m and Vmax. 1.8μmol/h per mg of protein. Treatment of the membranes with various detergents caused a preferential solubilization of protein compared with lipids. Membranes dissolved in sodium dodecyl sulphate or phenol–acetic acid–urea were subjected to polyacrylamide-gel electrophoresis at alkaline and acid pH respectively. The electrophoretic patterns given by the proteins of the chromaffin granule membrane were distinct from those given by the chromogranins, and from those given by mitochondrial and microsomal membrane proteins.


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