Por favor, use este identificador para citar o enlazar este ítem: http://repositorio.ufc.br/handle/riufc/59839
Tipo: Artigo de Periódico
Título : cDNA cloning and 1.75 A˚ crystal structure determination of PPL2, an endochitinase and N-acetylglucosaminebinding hemagglutinin from Parkia platycephala seeds
Título en inglés: cDNA cloning and 1.75 A˚ crystal structure determination of PPL2, an endochitinase and N-acetylglucosaminebinding hemagglutinin from Parkia platycephala seeds
Autor : Cavada, Benildo S.
Moreno, Frederico B. B.
Rocha, Bruno A. M. da
Azevedo Júnior4, Walter F. de
Rádis-Baptista, Gandhi
Palabras clave : Análise química;Toxinas
Fecha de publicación : 2006
Editorial : The FASEB Journal express
Citación : CAVADA, Benildo S.; MORENO, Frederico B. B.; ROCHA, Bruno A. M. da; AZEVEDO JÚNIOR, Walter F. de; RÁDIS-BAPTISTA, Ghandi., et al. cDNA cloning and 1.75 A˚ crystal structure determination of PPL2, an endochitinase and N-acetylglucosaminebinding hemagglutinin from Parkia platycephala seeds. The FASEB Journal express, United States, v. 273, p. 3962–3974. 2006.
Abstract: Parkia platycephala lectin 2 was purified from Parkia platycephala (Leguminosae, Mimosoideae) seeds by affinity chromatography and RP-HPLC. Equilibrium sedimentation and MS showed that Parkia platycephala lectin 2 is a nonglycosylated monomeric protein of molecular mass 29 407 ± 15 Da, which contains six cysteine residues engaged in the formation of three intramolecular disulfide bonds. Parkia platycephala lectin 2 agglutinated rabbit erythrocytes, and this activity was specifically inhibited by N-acetylglucosamine. In addition, Parkia platycephala lectin 2 hydrolyzed b(1–4) glycosidic bonds linking 2-acetoamido-2-deoxy-b-d-glucopyranose units in chitin. The full-length amino acid sequence of Parkia platycephala lectin 2, determined by N-terminal sequencing and cDNA cloning, and its three-dimensional structure, established by X-ray crystallography at 1.75 A˚ resolution, showed that Parkia platycephala lectin 2 is homologous to endochitinases of the glycosyl hydrolase family 18, which share the (ba)8 barrel topology harboring the catalytic residues Asp125, Glu127, and Tyr182.
URI : http://www.repositorio.ufc.br/handle/riufc/59839
ISSN : 0892-6638
Aparece en las colecciones: LABOMAR - Artigos publicados em revistas científicas

Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
2006_art_bscavada.pdf594,41 kBAdobe PDFVisualizar/Abrir


Los ítems de DSpace están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.