Induction of phenolic acids and metals in Arachis hypogaea L. plants due to feeding of three lepidopteran pests

The feeding of lepidopteran pests, Amsacta albistriga W., Aproaerema modicella D. and Spilosoma obliqua W., caused feeding stress in the Arachis hypogaea L. plants. As a common defensive response, the plant exhibited variations in the primary and secondary metabolic contents. Groundnut plant antioxidative enzymes such as peroxidase, superoxide dismutase, polyphenol oxidase, catalase and phenyl ammonia lyase exhibited alterations to confer resistance against the pest. Phenolic compounds, namely coumaric acid, chlorogenic acid, resveratrol, epicatechin, ferulic acid and caffeic acid, showed active defensive role in groundnut plant against the pest feeding through their significant presence in Fourier transform infrared spectroscopy, high-performance liquid chromatography and gas chromatography studies. Changes in metal contents like iron, magnesium, zinc, potassium and calcium were also reported through atomic absorption studies, indicating their defensive role against the biotic stress caused on groundnut by the three lepidopteran pests. The present study can further assist in recognizing the importance of these specific phenolic acids and metals of groundnut in its pest management.     

Characterization of antibodies to chicken riboflavin carrier protein: Antigenicity of the tryptic fragments

The antigenecity of tryptic fragments of reduced and carboxymethylated chicken riboflavin carrier protein were studied. The tryptic sites of the native riboflavin carrier protein bound to riboflavin were inaccessible. The molecular weight and the elution profile on high performance liquid chromatography (TSK 545 DEAE) were unaltered at an enzyme to substrate ratio of 1:31. However, carboxymethylated riboflavin carrier protein could be cleaved into 3 or 4 fragments at an enzyme to substrate ratio of 1:250 or 1:125. Chromatographic separation of the tryptic fragments on high pressure liquid chromatography (TSK 545 DEAE) revealed the presence of two fragments with different elution profiles but similar molecular weight 26 ±2 kDa. Only one fragment (associated with peak 2) had the ability to displace chicken riboflavin carrier protein in an homologous chicken riboflavin carrier protein radioimmunoassay. Thus, carboxymethylated ribotlavin carrier protein which does not compete with chicken riboflavin carrier protein in the radioimmunoassay, on mild trypsinization generates a fragment which interacts with chicken riboflavin carrier protein in radioimmunoassay.