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Chaudhary Sarwan Kumar Himachal Pradesh Agriculture University, Palampur

Himachal Pradesh Krishi Vishvavidyalaya (renamed as Chaudhary Sarwan Kumar Himachal Pradesh Krishi Vishvavidyalaya in June, 2001) was established on 1st November, 1978.The College of Agriculture (established in May, 1966) formed the nucleus of the new farm University. It is ICAR accredited and ISO 9001:2015 certified institution. The Indian Council of Agricultural Research has ranked this University at eleventh place among all farm universities of the country. The University has been given the mandate for making provision for imparting education in agriculture and other allied branches of learning, furthering the advancement of learning and prosecution of research and undertaking extension of such sciences, especially to the rural people of Himachal Pradesh. Over the years, this University has contributed significantly in transforming the farm scenario of Himachal Pradesh. It has developed human resources, varieties and technologies and transferred these to farming community enabling the State to receive the “Krishikarman award” of Govt. of India four times in row for food grain production among small states of the country. Today, the State has earned its name for hill agricultural diversification and the farming community has imposed its faith in the University.

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  • ThesisItemOpen Access
    ISOLATION AND PURIFICATION OF LECTINS FROM VIGNA SPECIES
    (CSKHPKV, Palampur, 2015-07-13) Tripathi, Ankur; Katoch, Rajan
    In the present investigation, seeds of five Vigna species were investigated for hemagglutinating activity against human and rabbit erythrocytes. The seed extracts of Vigna mungo and Vigna radiata showed agglutination activity with human as well as rabbit erythrocytes, whereas Vigna unguiculata, Vigna umbellata and Vigna angularis exhibited agglutination only with trypsinized rabbit erythrocytes. Among the various tested sugars, agglutination activity was best inhibited by D-galactose. Vigna radiata extract exhibited a higher level of agglutination with rabbit erythrocytes and was selected for isolation and purification of lectin. Lectin was purified by employing a protocol that entailed ion exchange, gel filtration and affinity chromatography with 192.47 fold purification and 73.14 (HU/mg) specific activity. Under reducing conditions purified lectin was found to be a monomer with 25.0kDa molecular weight. Maximum agglutination activity of purified lectin was observed at pH 5.0 with (98%) stability and maintained steadily between pH 6-9. Maximum agglutination activity was observed at 370C (68.76%) and minimum at 650C where agglutination activity was completely lost. Agglutination activity was readily inhibited by D-galactose at 3.12mM. Lectins, due to various biological properties have a potential in pest control and plant defense. Their high level expression can confer resistance to a wide range of insects and could be exploited for crop improvement.