Consulta: subjectFacets:"Agglutinin"
Registros recuperados: 2
Data/hora: 06/06/2024 19:09:10

Analysis of castor bean ribosome-inactivating proteins and their gene expression during seed development
Provedor de dados: 74
Autores: Loss-Morais,Guilherme; Turchetto-Zolet,Andreia Carina; Etges,Matheus; Cagliari,Alexandro; Körbes,Ana Paula; Maraschin,Felipe dos Santos; Margis-Pinheiro,Márcia; Margis,Rogério.
Ribosome-inactivating proteins (RIPs) are enzymes that inhibit protein synthesis after depurination of a specific adenine in rRNA. The RIP family members are classified as type I RIPs that contain an RNA-N-glycosidase domain and type II RIPs that contain a lectin domain (B chain) in addition to the glycosidase domain (A chain). In this work, we identified 30 new plant RIPs and characterized 18 Ricinus communis RIPs. Phylogenetic and functional divergence analyses indicated that the emergence of type I and II RIPs probably occurred before the monocot/eudicot split. We also report the expression profiles of 18 castor bean genes, including those for ricin and agglutinin, in five seed stages as assessed by quantitative PCR. Ricin and agglutinin were the most...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Agglutinin; Evolution; Lipase; Ricinus communis; Ricin; RIPs.
Ano: 2013
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572013000100011

Purification and characterisation of a lectin from the red marine alga Pterocladiella capillacea (S.G. Gmel.) Santel. &amp;amp; Hommers.
Provedor de dados: 88
Autores: OLIVEIRA,STÉLIO R.M.; NASCIMENTO,ANTONIA E.; LIMA,MARIA E.P.; LEITE,YÁSKARA F.M.M.; BENEVIDES,NORMA M.B.
A lectin present in the marine red alga Pterocladiella capillacea was purified and characterised by extraction of soluble proteins (crude extract) in 20 mM Tris-HCl buffer, pH 7.5. Among the analysed erythrocytes (human blood group A, B and O and the animals ox, goat, chicken and rabbit) the lectin agglutinated specifically rabbit erythrocytes. The hemagglutinating activity assay showed that the lectin was not dependent on divalent cations and was shown to be inhibited by the glycoproteins avidin and mucin. The purification procedure was conduced by precipitation of the crude extract with 80% saturation ammonium sulfate (F0/80) followed by affinity chromatography on guar-gum column. The lectin of P. capillacea was purified 14.5 fold and had a recovery of...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Agglutinin; Algae; Lectin; Pterocladiella capillacea; Purification.
Ano: 2002
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-84042002012000003