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1.
Article in English | IMSEAR | ID: sea-168054

ABSTRACT

Correlation coefficient and path analysis studies were carried out with seventeen parents (fourteen lines and three testers) resulting 42 F1 crosses for fifteen yield contributing component characters. The phenotypic and genotypic correlation analysis revealed that seed yield was highly significantly and positively correlated with number of branches, number of clusters, number of pods per plant, number of seeds per plant pod weight, total biomass and also highly significantly and positively correlated among themselves. Path coefficient analysis for seed yield revealed that significant phenotypic and genotypic direct effect with seeds per plant, 100 seed weight, harvest index, pod weight and number of clusters per plant. Hence selection for these characters may be carried out in the field and lab for overall yield improvement in blackgram.

2.
Article in English | IMSEAR | ID: sea-162268

ABSTRACT

Correlation coefficient and path analysis studies was conducted with eight parents and their 28 F1 crosses for twelve component characters including seed yield and revealed significant positive association of pods per plant, harvest index and clusters per plant with seed yield in parental generation whereas in F1 generation, significant positive association of clusters per plant, pods per plant, days to maturity, days to 50% flowering, pods per cluster and 100-seed weight with seed yield was observed. Further, it was found that number of seeds per pod, harvest index, pods per plant and number of primary branches per plant showed high positive direct effects on seed yield in parents whereas in crosses, seeds per pod, pods per plant, harvest index and days to maturity showed high positive direct effect on seed yield. Hence selection based on these traits would be effective in increasing the seed yield.

3.
J Biosci ; 1997 Sep; 22(4): 439-455
Article in English | IMSEAR | ID: sea-161138

ABSTRACT

Blackgram (Vigna mungo L. Hepper) seeds contain two galactose-specific lectins, BGL-I and BGL-II. BGL-I was partially purified into two monomeric lectins which were designated as BGL-I-1 (94 kDa) and BGL-I-2 (89 kDa). BGL-II is a monomeric lectin of 83 kDA. The purified lectins were associated with galactosidase activities. BGL-I-1 and BGL-II were copurified with α-galactosidase activity while BGL-I-2 was largely associated with β-galactosidase activity. These lectins agglutinate trypsin treated rabbit erythrocytes, but not the human erythrocytes of A, B or O groups. They were stable between pH 3·5 and 7·5 for their agglutination. The lectins did not show any metalion requirement. They were inactivated at 50°C. The lectin activity was inhibited by D-galactose (0·1 mM). The Scatchard plots of galactose binding to these lectins are nonlinear and biphasic curves indicative of multiple binding sites. The data show that the monomeric lectins have both lectin and galactosidase activities suggestive of a bifunctional protein.

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