Please use this identifier to cite or link to this item: http://nopr.niscpr.res.in/handle/123456789/15294
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dc.contributor.authorSuseelan, K N-
dc.contributor.authorSainis, K B-
dc.contributor.authorMitra, R-
dc.date.accessioned2012-12-24T19:13:36Z-
dc.date.available2012-12-24T19:13:36Z-
dc.date.issued2001-06-
dc.identifier.issn0975-0959 (Online); 0301-1208 (Print)-
dc.identifier.urihttp://hdl.handle.net/123456789/15294-
dc.description193-198en_US
dc.description.abstractA 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.en_US
dc.language.isoen_USen_US
dc.publisherNISCAIR-CSIR, Indiaen_US
dc.rights CC Attribution-Noncommercial-No Derivative Works 2.5 Indiaen_US
dc.sourceIJBB Vol.38(3) [June 2001]en_US
dc.titleCharacterization and biological activities of Chenopodium leaf hemagglutinin (CLH)en_US
dc.typeArticleen_US
Appears in Collections:IJBB Vol.38(3) [June 2001]

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