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[null,"1.","Record Nr.",null,"UNINA9910624369903321"]
[null,null,"Autore",null,"Huarachi-Valencia Juan-Pablo"]
[null,null,"Titolo",null,"Aislamiento, actividad biológica y caracterización bioquímica de lectina de semillas de chenopodium quinoa willd. (cv. Salcedo-INIA)"]
[null,null,"Pubbl/distr/stampa",null,"Puno : , : Instituto Universitario de Innovación Ciencia y Tecnología Inudi Perú, , 2022"]
[null,null,"Descrizione fisica",null,"1 electronic resource (88 pages)"]
[null,null,"Soggetti",null,"Earth sciences"]
[{"$nulls":4},"Geography"]
[{"$nulls":4},"Environmental protection - Planning"]
[null,null,"Lingua di pubblicazione",null,"Spagnolo"]
[null,null,"Formato",null,"Materiale a stampa"]
[null,null,null,"Livello bibliografico","Monografia"]
[null,null,null,"Sommario/riassunto","Lectins act as cell recognition molecules, and probably in plant defense. The CqLEC, lectin from Ch. quinoa cv Salcedo INIA, was isolated, purified and characterized from 70 g of seeds through saline extraction, and the combination of two molecular exclusion chromatographies such as Sephadex G-100 and G -75, obtaining 5.53 mg/ml of protein with hemagglutinating activity, as well as by reverse phase HPLC at 32 minutes with 54% buffer B, indicating that it had a low number of hydrophobic residues in its structure. Likewise, SDS-PAGE showed that the purified lectin was homogeneous since it had a single component corresponding to a 12.82 kDa protein. Being that the CqLEC agglutinated human erythrocytes of the “O Rh+” blood group with an MHC of 1.95 μg/ml, inhibited by fucose (0.78 mM) and the chelating agent EGTA (0.1 mM), this indicated that would be a fucose-binding lectin dependent on divalent ions such as calcium or manganese. On the other hand, this protein showed specific bactoagglutination for E. coli (CMB equal to 200 μg/ml), as well as insecticidal activity against Symmetrischema plaesiosema larvae (1000 ppm of CqLEC, P < 0.05). Complete amino acid analysis revealed that CqLEC is an acidic lectin (70.54% hydrophilic residues and 29.46% hydrophobic residues), with glutamic acid (33%) prevailing, with a molecular mass of 12.859 kDa. By sequential homology study, it was determined that it belongs to the family of vegetable lectins of "]
[{"$nulls":4},"Legumes, showing 82.1% similarity with the precursor of agglutinin I extracted from the bark of Cladrastis kentukea. The CqLEC also presented highly conserved residues in its structure, such as Leu 4, Ser 6 and Phe 7."]
[{"$nulls":4},"Las lectinas actúan como moléculas de reconocimiento celular, y probablemente en la defensa vegetal. La CqLEC, lectina de Ch. quinoa cv Salcedo INIA, fue aislada, purificada y caracterizada a partir de 70 g de semillas a través de extracción salina, y la combinación de dos cromatografías de exclusión molecular tales como las de Sephadex G-100 y G-75 logrando obtenerse 5,53 mg/ml de proteína con actividad hemaglutinante, así como por HPLC de fase reversa a los 32 minutos con 54 % de tampón B indicando que poseía un bajo número de residuos hidrofóbicos en su estructura. Asimismo, el SDS-PAGE demostró que la lectina purificada fue homogénea ya que presentaba un solo componente correspondiente a una proteína de 12,82 kDa. Siendo que la CqLEC aglutinó eritrocitos humanos del grupo sanguíneo “O Rh+” con una CMH de 1,95 mg/ml, inhibido por fucosa (0,78 mM) y el agente quelante EGTA (0,1 mM), esto indicaba que sería una lectina ligadora de fucosa dependiente de iones divalentes tales como el calcio o el manganeso. Por otra parte, esta proteína mostró una bactoaglutinación específica para E. coli (CMB igual a 200 mg/ml), así como actividad insecticida en contra de larvas de Symmetrischema plaesiosema (1000 ppm of CqLEC, P < 0,05). El análisis completo de aminoácidos reveló que la CqLEC es una lectina de naturaleza ácida (70,54 % de residuos hidrofílicos y 29,46 % de residuos hidrofóbicos), prevaleciendo el ácido glutámico (33 %), con una masa molecular de 12,859 kDa. Por estudio de homología secuencial se determinó que ésta pertenece a la familia de lectinas vegetales de Leguminosas, mostrando 82,1 % de similitud con el precursor de la aglutinina I extraída a partir de la corteza de Cladrastis kentukea. La CqLEC también presentó residuos altamente conservados en su estructura tales como Leu 4, Ser 6 y Phe 7."]