Evaluation of thermal behavior of latex membranes from genetically improved rubber tree (Hevea brasiliensis)

Thermal stability, thermal decomposition process, residual mass, temperature of glass transition (T-g) and temperature dependence of storage modulus (E'), were determined for latex membranes prepared from six clones of Hevea brasiliensis: IAC 331, IAC 332, IAC 333 and IAC 334 grown at experimental plantations of Instituto Agronomico de Campinas (IAC) in Votuporanga, São Paulo State, Brazil. Latex membranes from GT1 and RRIM 600 Asian matrix clones were used as references. The thermal behavior of latex membranes from genetically improved rubber trees was characterized using thermogravimetry/derivative thermogravimetry (TG/DTG), differential scanning calorimetry (DSC) and dynamic mechanical analysis (DMA). The thermal behavior of latex from clones studied in the present work showed similar features of the clones previously reported (IAC 40, IAC 300, IAC 301, IAC 328, IAC 329 and IAC 330), with mass loss in four consecutive steps, except IAC 333, which showed an additional mass loss step. (c) 2006 Elsevier B.V. All rights reserved.

The influence of natural rubber/Au nanoparticle membranes on the physiology of Leishmania brasiliensis

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Characterization of Paracoccidioides brasiliensis PbDfg5p, a cell-wall protein implicated in filamentous growth

The dimorphic fungus Paracoccidioides brasiliensis is the causative agent of the most frequent systemic mycosis in Latin America. In humans, infection starts by inhalation of fungal propagules, which reach the pulmonary epithelium and differentiate into the yeast parasitic phase. Here we describe the characterization of a Dfg5p ((d) under bar efective for (f) under bar ilamentous (g) under bar rowth) homologue of P. brasiliensis, a predictable cell wall protein, first identified in Saccharomyces cerevisiae. The protein, the cDNA and genomic sequences were analysed. The cloned cDNA was expressed in Escherichia coli and the purified rPbDfg5p was used to obtain polyclonal antibodies. Immunoelectron microscopy and biochemical studies demonstrated the presence of PbDfg5p in the fungal cell wall. Enzymatic treatments identified PbDfg5p as a beta-glucan linked protein that undergoes N -glycosylation. The rPbDfg5p bound to extracellular matrix components, indicating that those interactions could be important for initial steps leading to P. brasiliensis attachment and colonization of host tissues. The P. brasiliensis dfg5 nucleotide and deduced protein, PbDfg5p, sequences reported in this paper had been submitted to the GenBank database under Accession Nos AY307855 (cDNA) and DQ534495 (genomic). Copyright (C) 2007 John Wiley & Sons, Ltd.

Altered Ex Vivo Expression of Caspase 8, Caspase 9, and Bcl-2 Is Associated with T-Cell Hyporeactivity in Patients with Paracoccidioidomycosis

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Enolase from Paracoccidioides brasiliensis: isolation and identification as a fibronectin-binding protein

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Phylogeny of Triatoma sherlocki (Hemiptera: Reduviidae: Triatominae) Inferred from Two Mitochondrial Genes Suggests Its Location Within the Triatoma brasiliensis Complex

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)