Characterization and biological activities of Chenopodium leaf hemagglutinin (CLH).
A hemagglutinin (CLH) having native molecular mass of 58 kDa and subunit molecular mass of 33 kDa had been purified from the 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. The N-terminal amino acid sequence analysis showed that CLH had no homology with any of the plant hemagglutinins studied so far. It was inactive towards human peripheral blood cells but mitogenic for mouse spleen B-lymphocytes. CLH inhibited protein synthesis in rat thymocytes at high concentration. CLH did not inhibit TMV infection of leaves indicating absence of antiviral properties.
Suseelan
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KN
Nuclear Agriculture and Biotechnology Division, Bhabha Atomic Research Centre, Mumbai, India. nad@magnum.barc.ernet.in
Sainis
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KB
Mitra
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D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D001224:Aspartic Acid / Q000737:chemistry; D002449:Cell Aggregation; D027462:Chenopodium / Q000737:chemistry*; D004305:Dose-Response Relationship, Drug; D004912:Erythrocytes / Q000378:metabolism; D018698:Glutamic Acid / Q000737:chemistry; D005998:Glycine / Q000737:chemistry; D006388:Hemagglutinins / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D008239:Lysine / Q000737:chemistry; D008715:Methionine / Q000737:chemistry; D051379:Mice; D010649:Phenylalanine / Q000737:chemistry; D018515:Plant Leaves / Q000737:chemistry*; D011817:Rabbits; D051381:Rats; D013154:Spleen / Q000378:metabolism; D013950:Thymus Gland / Q000166:cytology; D014364:Tryptophan / Q000737:chemistry
D000596:Amino Acids; D006388:Hemagglutinins; D001224:Aspartic Acid; D018698:Glutamic Acid; D010649:Phenylalanine; D014364:Tryptophan; D008715:Methionine; D008239:Lysine; D005998:Glycine