RESUMO
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.
Assuntos
Aminoácidos/química , Animais , Ácido Aspártico/química , Agregação Celular , Chenopodium/química , Relação Dose-Resposta a Droga , Eritrócitos/metabolismo , Ácido Glutâmico/química , Glicina/química , Hemaglutininas/química , Lisina/química , Metionina/química , Camundongos , Fenilalanina/química , Folhas de Planta/química , Coelhos , Ratos , Baço/metabolismo , Timo/citologia , Triptofano/químicaRESUMO
A hemagglutinin was isolated and purified from the leaves of Chenopodium (Chenopodium amaranticolor) using ion-exchange chromatography and affinity chromatography on fetuin-agarose matrix. It agglutinated rabbit erythrocytes. The hemagglutinin had a native molecular mass of 58 kDa, as estimated by gel filtration and showed a single band of molecular mass of 33 kDa on SDS-PAGE. It showed hemagglutination activity over the pH range 3-12 and was found to be stable up to 70 degrees C. On isoelectrofocussing, the pI of this hemagglutinin was estimated to be 5.25. However, it was found to contain seven charge variants when isoelectrofocussing was performed in presence of 6M urea.
Assuntos
Chenopodium/química , Cromatografia em Gel , Cromatografia por Troca Iônica , Eletroforese em Gel de Poliacrilamida , Hemaglutininas/química , Concentração de Íons de Hidrogênio , Focalização Isoelétrica , Ligantes , Folhas de Planta/química , Ligação Proteica , Temperatura , Fatores de TempoRESUMO
Blackgram (Vigna mungo L. Hepper) seeds contain two galactose-specific lectins, BGL-I and BGL-II. BGL-I was partially purified into two monomeric lectins which were designated as BGL-I-1 (94 kDa) and BGL-I-2 (89 kDa). BGL-II is a monomeric lectin of 83 kDA. The purified lectins were associated with galactosidase activities. BGL-I-1 and BGL-II were copurified with α-galactosidase activity while BGL-I-2 was largely associated with β-galactosidase activity. These lectins agglutinate trypsin treated rabbit erythrocytes, but not the human erythrocytes of A, B or O groups. They were stable between pH 3·5 and 7·5 for their agglutination. The lectins did not show any metalion requirement. They were inactivated at 50°C. The lectin activity was inhibited by D-galactose (0·1 mM). The Scatchard plots of galactose binding to these lectins are nonlinear and biphasic curves indicative of multiple binding sites. The data show that the monomeric lectins have both lectin and galactosidase activities suggestive of a bifunctional protein.