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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Purification, primary structure and potential functions of a novel lectin from Bauhinia forficata seeds

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Author(s):
Silva, Mariana C. C. [1] ; Santana, Lucimeire A. [1] ; Mentele, Reinhard [2, 3] ; Ferreira, Rodrigo S. [1] ; de Miranda, Antonio [4] ; Silva-Lucca, Rosemeire A. [5] ; Sampaio, Misako U. [1] ; Correia, Maria T. S. [6] ; Oliva, Maria L. V. [1]
Total Authors: 9
Affiliation:
[1] Univ Fed Sao Paulo, Dept Bioquim, BR-04044020 Sao Paulo - Brazil
[2] Inst Clin Neuroimmunol LMU, Munich - Germany
[3] Max Planck Inst Biochem, Dept Prot Analyt, D-82152 Martinsried - Germany
[4] Univ Fed Sao Paulo, Dept Biofis, BR-04044020 Sao Paulo - Brazil
[5] Univ Estadual Oeste Parana, Ctr Engn & Ciencias Exatas, BR-85903000 Toledo, PR - Brazil
[6] Univ Fed Pernambuco, Dept Bioquim, BR-50670901 Recife, PE - Brazil
Total Affiliations: 6
Document type: Journal article
Source: Process Biochemistry; v. 47, n. 7, p. 1049-1059, JUL 2012.
Web of Science Citations: 20
Abstract

A new lectin. Bfl. was purified from Bauhinia forficata seeds by ammonium sulfate fractionation. DEAE-Sephadex ion exchange chromatography, Sepharose-4B and chitin affinity chromatographies and Superdex 75 size exclusion chromatography. The molecular homogeneity and purity of BfL were assessed by reversed-phase H PLC. BfL appeared as a single band of approximately 27.0 kDa on SDS-PAGE under non-reducing and reducing conditions, and its molecular weight was determined to be 27,850 Da by LC/ESI-MS. Bit is a glycoprotein with a carbohydrate content of 6.24% determined by the phenol-sulfuric acid method. Fetuin, asialofetuin, thyroglobulin and azocasein inhibited the hemagglutinating activity of BfL, whereas saccharides did not. Bfl hemagglutinating activity was stable at 100 degrees C for 30 min, pH-dependent, with the highest activity at pH 6.0, and metal-independent. The primary structure of BfL shows similarity with other lectins from the genus Bauhinia. Deconvolution of the BfL circular dichroism (CD) spectrum indicated the presence of alpha-helix and beta structures. BfL increases coagulation time, but this effect is not related to human plasma kallikrein or human factor Xa inhibition. Bfl also inhibits ADP- and epinephrine-induced platelet aggregation in a dose-dependent manner and is the only currently described lectin from Bauhinia that exhibits anticoagulant and antiplatelet aggregating properties. (c) 2012 Elsevier Ltd. All rights reserved. (AU)

FAPESP's process: 09/53766-5 - Proteins from plant source with selectivity for inhibition of mammalian enzymes and their role as an anti-inflammatory, antithrombotic, anti-diabetic and anti-tumor agent
Grantee:Maria Luiza Vilela Oliva
Support Opportunities: Research Projects - Thematic Grants