Please use this identifier to cite or link to this item: http://nopr.niscpr.res.in/handle/123456789/15294
Title: Characterization and biological activities of Chenopodium leaf hemagglutinin (CLH)
Authors: Suseelan, K N
Sainis, K B
Mitra, R
Issue Date: Jun-2001
Publisher: NISCAIR-CSIR, India
Abstract: A hemagglutinin (CLH) having native molecular mass of 58 kDa and subunit  molecular mass of 33 kDa had been purified from thc leaves of Chenopodium amaranticolor. The protein agglutinated rabbit erythrocytes and no agglutination was observed with any of the groups A, B or O of human blood. The amino acid composition revealed that CLH was rich in aspartic acid, glutamic acid, glycine and phenylalanine and also significant amount of methionine. Thc N-terminal amino acid sequence analysis showed that CLH had no homology with any of the plant hcmagglutinins studied so far. It was in active towards human peripheral blood cells but mitogenic for mouse spleen B-Iymphocytes. CLH inhibited protein synthesis in rat thymocytes at high concentration. CLH did not inhibit TMV infection of leaves indicating absence of antiviral properties.
Page(s): 193-198
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections:IJBB Vol.38(3) [June 2001]

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