Sabiia Seb
PortuguêsEspañolEnglish
Embrapa
        Busca avançada

Botão Atualizar


Botão Atualizar

Ordenar por: 

RelevânciaAutorTítuloAnoImprime registros no formato resumido
Registros recuperados: 2
Primeira ... 1 ... Última
Imagem não selecionada

Imprime registro no formato completo
Interaction of antimicrobial peptide Plantaricin149a and four analogs with lipid bilayers and bacterial membranes BJM
Lopes,José Luiz de Souza; Hissa,Denise Cavalcante; Melo,Vânia Maria Maciel; Beltramini,Leila Maria.
The amidated analog of Plantaricin149, an antimicrobial peptide from Lactobacillus plantarum NRIC 149, directly interacts with negatively charged liposomes and bacterial membranes, leading to their lysis. In this study, four Pln149-analogs were synthesized with different hydrophobic groups at their N-terminus with the goal of evaluating the effect of the modifications at this region in the peptide's antimicrobial properties. The interaction of these peptides with membrane models, surface activity, their hemolytic effect on red blood cells, and antibacterial activity against microorganisms were evaluated. The analogs presented similar action of Plantaricin149a; three of them with no hemolytic effect (< 5%) until 0.5 mM, in addition to the induction of a...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Antimicrobial activity antimicrobial peptide calcein leakage; Hemolytic assay.
Ano: 2013 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822013000400038
Imagem não selecionada

Imprime registro no formato completo
Purification and partial characterization of a lectin from Caesalpinia tinctoria Domb, ex Dc fruits Braz. J. Plant Physiol.
Oliveira,Marli Lourdes de; Beltramini,Leila Maria; Simone,Salvatore Giovanni de; Brumano,Maria Helena Nasser; Silva-Lucca,Rosemeire Aparecida; Nakaema,Marcelo Kiyoshi Kian; Pires,Christiano Vieira; Oliveira,Maria Goreti de Almeida.
A lectin was isolated from the pod saline extract of Caesalpinia tinctoria by dialoconcentration on Centripep-10 and affinity chromatography on chitin column. The purified lectin was partially characterized with respect to its biochemical and structural properties. It contains 8.3 % of carbohydrate and exhibited an agglutinating activity against human erythrocytes (ABO groups). Its amino acid composition was characterized by a great number of acidic and hydrophobic residues and the estimated molecular mass was 12.5 kDa. The presence of only one N-terminal amino acid sequence (D¹-V-P-A-Y-V-Y-V-H-F10-G-F-G-E-E-H-R -D-V-F20-D), showed the homogeneity of the purified lectin. The far-ultraviolet circular dichroism (CD) spectrum of lectin indicated that it...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Circular dichroism; Leguminosae; Plant defense; Pod; Secondary structure.
Ano: 2003 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1677-04202003000200008
Registros recuperados: 2
Primeira ... 1 ... Última
 

Empresa Brasileira de Pesquisa Agropecuária - Embrapa
Todos os direitos reservados, conforme Lei n° 9.610
Política de Privacidade
Área restrita

Embrapa
Parque Estação Biológica - PqEB s/n°
Brasília, DF - Brasil - CEP 70770-901
Fone: (61) 3448-4433 - Fax: (61) 3448-4890 / 3448-4891 SAC: https://www.embrapa.br/fale-conosco

Valid HTML 4.01 Transitional