137 resultados para calc alkaline rock
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The Brazilian Granitic Province from southeastern Mato Grosso do Sul and Mato Grosso region, central western Brazil, can be divided into two major groups and/or magmatic events related to the evolution of the Paraguay Fold Belt. The southern portion crops out in Mato Grosso do Sul State and is constituted by the Taboco, Rio Negro, Coxim and Sonora massifs forming NE-SW oriented, elongated small intrusions. The north portion crops out in Mato Grosso State and is constituted by the São Vicente, Araguaiana and Lajinha batholiths. Lithogeochemical aspects of the northern granites point to Type-I granites ranging from K calc-alkaline to high-K, peraluminous to metaluminous in composition, generated in an environment of continental collision and/or post- collision decompression. The southern granites are Type-I, from K calc-alkaline to high-K, peraluminous to subordinate metalummous, in a syn-collision continental arc environment with the exception of some pre-collisional facies from the Rio Negro Massif. The southern granites have less SiO 2 and K 2O, and are less differentiated and evolved than granites from the northern region. The four southern granites can be grouped into two subordinate sets with the degree of differentiation increasing from South (Taboco and Rio Negro) to North (Coxim and Sonora). The granitic rocks are characterized by a magmatism generated by melting of material from the lower crust which suggests that in this province the formation from non-cogenetic magmas with diversified compositions and distinct degrees of fractioning reaching more steady consolidated environments at the end of the collisional event in the southeastern Amazonian Craton.
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The Neoproterozoic granitogenesis related to the Central Mantiqueira Province comprise the calc alkaline to alkaline granitoid complexes of Sorocaba, San Francisco, São Roque, Ibiúna and Piedade. These complexes occur in a ruptil tectonic to tardi (Sn+3) event. The emplacement of the different facies in transtractives structures of the pull-apart type are characterized in the area by the main transcurrent shear zones of Taxaquara-Pirapora, Itu-Jundiuvira, Moreiras, Cangüera and Caucáia of ENE-WSW general direction. The massifs present complex internal architecture characterized by intrusions in restrict initial phase of intermediate equigranular nature. Also present a main phase of porfiroid monzo and sienogranite that fragments the previous phase, followed by lateral accretion of equi to inequigranular material, and in some cases by the accretion of late phases of circular bodies of porfiroid rapakivi granites, and a late to final phase of aplitic to pegmatitic composition. This magmatism grew with the intrusions of successive magmatic pulses, partially controlled by many reactivations of the shear zones. The REE also suggest that the magmatic phases are similar, synchronous and repetitive in four of the complexes in both domains, present in the São Francisco Complex. The crystallization starts from accretion processes, but compositionally quite different from the others. The variation in compositions and ages (TDM) for these granites reflect the derivation from different sources developed under different magmatic conditions, followed by processes of contamination that frequently occur in the crust.
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The Rio Apa Massif corresponds to the southeastern portion of the Amazonian Craton and crops out in the Mato Grosso do Sul State, Brazil. It is constituted by rocks of paleoproterozoic age of Rio Apa Complex, Alto Tererê Group and the plutonic-volcanic suites of the Amoguijá Group, subdivided in Alumiador Intrusive suits and Serra da Bocaina Volcanic. The Volcanic Suite is represented by São Francisco and Bocaina mountains and is constituted by terms of the composition of alkali - rhyolitic to rhyolitic, including in minor amounts riodacite, andesite and dacite. It consists of a variety of textual subvolcanic rocks, volcanic and varied volcanoclastics. The pyroclastic deposits are very expressive and consist of pyroclastic particle immerse in aphanitic matrix, fine grained or amorphous, where quartz, feldspar, chlorite, sericite, microlithes of carbonate, sparse spherulites and reliquiar volcanic glass can be distinguished. The pyroclastic rocks are represented by breccias, ignimbrites, agglomerate, tuffs, lapillistones and pumices and contain commonly vitroclasts, lithoclasts and crystalloclasts, pumices, fiammes, glass shards, spherulites, vesicles and amygdales. They are calc-alkaline rocks with dominant peraluminous character high to middle potassium series and define a sin-colisional dominant tectonic and are genetically associated to the evolution of the Amoguijá Magmatic Arc.
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Rio Branco Rapakivi Batholith is located on the southwestern portion of the Amazonian Craton in Mato Grosso and belongs to the Cachoeirinha Tectonic Domain, part of the Rio Negro-Juruena Geochronological Province, Central Brasil. The batholith is constituted by microgabbros to quartz microgabbros and microdiorites to quartz microdiorites, middle to fine-grained equigranular to porphyritic varieties form the Rio Branco Intrusive Basic Suite, showing a discontinuous distribution and located near the margins of the intrusion.Majorly constituted by porphyritic, granophyric and isotropic facies of Rio Branco Intrusive Acid Suit which is composed by older dark red rapakivi monzogranites to quartz monzonites and quartz sienites (1403±0.6 Ma) and the younger red rapakivi leuco-monzogranites (1382±49 Ma) and late equigranular to pegmatitic monzogranites. The magmatism is constituted by two distinct magmas related to the end of the collisional event of Cachoeirinha Orogeny, one with alkaline basalts generated in an intraplate environment and the other postorogenic to anorogenic with peraluminous to metaluminous compositions and define a high-K calc-alkaline to shoshonitic magmatism in transition among the I- and A-types. The contacts are marked by extensive mafic sills and dikes of alkaline basalts derived from intraplate environment of the Salto do Céu Intrusive Basic Suite (±808 Ma) associate to the Sunsás-Aguapei Orogenic Belt and metasedimentary rocks of the Aguapeí Grup.
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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
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Geological researches conducted in the past few years detected, through deep drill hole data, the presence of alkaline rocks in the region of Três Fontes-MG, where the Barbacena Group rocks, the Morro do Ferro Greenstone Belt rocks and Araxá/Canastra groups‟ rocks are exposed. This paper aimed the petrographic and chemical characterization of these alkaline rock types, which have not yet been described in the literature. Based on petrographic descriptions and geochemical and Scanning Electron Microscopy analysis, it was possible to characterize the rock in question as lamprophyre, rich in carbonates, phlogopite, pyroxene, olivine, titaniferous opaque minerals and apatite concentrations that reach 7%. This occurrence corresponds to an alkaline intrusion, which caused brecciation of host rocks, possibly indicating that the material is explosive, however, in the study area there was no evidence of volcanic activity on the surface
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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The Pluriserial Ribeira Magmatic System-590 of the Late Precambrian Ribeira Fold Belt comprises seven groups of high-K rocks of crustal or mantle origin with ages ranging between 620 and 570 Ma. One of these groups is represented by transalkaline suites akin to appinitic lamprophyres. The suites assemble one or more of following lithologies: (+/- quartz) gabbros and monzogabbros, (+/- quartz) diorites and monzodiorites, (+/- quartz) monzonites and syenites in addition to rare granites. All these rocks occur together in the Piracaia pluton, State of São Paulo. The mineralogy of the Piracaia suite comprises variable amounts of plagioclase (An 60-10), alkali-feldspars (orthoclase, microcline, albite), ortho- (Fe-hypersthene) and clinopyroxenes (augite), amphiboles (hornblende and rare late Fe-hastingsite), abundant biotite, quartz, opaques, sphene, allanite and zircon. Several magmatic pulses constructed the pluton. The Piracaia magma bulk trend evolved initially along the silica-undersaturation plane with simultaneous fractionation of accessory, mafic and felsic minerals. These are segregated in feldspar-rich cumulates. In the late stage, the evolutionary trend followed two distinct paths: one along the or-ab thermal barrier with the crystallization of syenites; the second one along the thermal valley in the or-ab-qz subsystem, producing quartz-syenites and granites. The source of the Piracaia magma was a 'vein-plus-wall-rock-system '. Together the pulses reflect increasing and decreasing participation of peridotites and mica pyroxenites, respectively, in the magmatogenic process. The magmatic pulses were stored in magma chambers, several drained by deep faults or fractures, which were successively reactivated and recharged. Each new pulse underwent mixing with earlier residual magma, followed by fractionation. During ascent through the hot and thickened post-collisional crust, the magma pulses underwent minor compositional changes by crustal contamination. The concentration of valuable elements (Cu, Zn, Gd) in the Piracaia pluton occurred during two phases of the magmatic evolution. Cu and Zn were enriched in cumulates and Gd was concentrated in residual quartz-syenitic veins. Due to their homogeneous dark colour and texture, the monzodiorites are exploited both for polished dimension stones and supports for sensitive scientific instruments. (C) 2001 Elsevier B.V. Ltd. All rights reserved.
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The alteration of minerals in rocks and the availability of elements for plant nutrition require long periods of time, and microorganisms are thought to induce the release of potassium and phosphate from rocks. In this context, this work evaluates the role of the yeast Torulaspora globosa, isolated from the sugar cane rhizosphere, in the solubilization of potassium from alkaline ultramafic rock powder. The experiments were performed in liquid medium, with or without agitation, at 30°C with the following treatments: culture medium + alkaline ultramafic; culture medium + yeast suspension; and culture medium + yeast suspension + alkaline ultramafic. The results showed that as much as 38% of the total potassium in the rock was released in the medium with the yeast during a 15-day period of incubation. Acid production may be the mechanism by which the yeast solubilizes potassium because the total acidity increased during the sampling period. Agitation (which increased oxygen availability) resulted in approximately 20% more biosolubilization of the alkaline ultramafic rock than with the static culture. These data indicate the potential for this yeast in biosolubilization processes and biofertilizer production.
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The aim of this study was to obtain membrane-bound alkaline phosphatase from osteoblastic-like cells of human alveolar bone. Cells were obtained by enzymatic digestion and maintained in primary culture in osteogenic medium until subconfluence. First passage cells were cultured in the same medium and at 7, 14, and 21 days, total protein content, collagen content, and alkaline phosphatase activity were evaluated. Bone-like nodule formation was evaluated at 21 days. Cells in primary culture at day 14 were washed with Tris-HCl buffer, and used to extract the membrane-bound alkaline phosphatase. Cells expressed osteoblastic phenotype. The apparent optimum pH for PNPP hydrolysis by the enzyme was pH 10.0. This enzyme also hydrolyzes ATP, ADP, fructose-1-phosphate, fructose-6-phosphate, pyrophosphate and beta-glycerophosphate. PNPPase activity was reduced by typical inhibitors of alkaline phosphatase. SDS-PAGE of membrane fraction showed a single band with activity of similar to 120 kDa that could be solubilized by phospholipase C or Polidocanol. (c) 2007 International Federation for Cell Biology. Published by Elsevier Ltd. All rights reserved.
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Pyrophosphatase activity of rat osseous plate alkaline phosphatase was studied at different concentrations of calcium and magnesium ions. with the aim of characterizing the modulation of enzyme activity by these metals. In the absence of metal ions, the enzyme hydrolysed pyrophosphate following Michaelian kinetics with a specific activity of 36.7 U/mg and K-0.5 = 88 mu M. In the presence of low concentrations (0.1 mM) of magnesium (or calcium) ions, the enzyme also exhibited Michaclian kinetics for the hydrolysis of pyrophosphate, but a significant increase in specific activity (123 U/mg) was observed. K-m values remained almost unchanged. Quite different behavior occurred in the presence of 2 mM magnesium (or calcium) ions. In addition to low-affinity sites (K-0.5 = 40 and 90 mu M, for magnesium and calcium, respectively), high-affinity sites were also observed with K-0.5 values 100-fold lower. The high-affinity sites observed in the presence of calcium ions represented about 10% of those observed for magnesium ions. This was correlated with the fact that only magnesium ions triggered conformational changes yielding a fully active enzyme. These results suggested that the enzyme could hydrolyse pyrophosphate, even at physiological concentrations (4 mu M), since magnesium concentrations are high enough to trigger conformational changes increasing the enzyme activity. A model, suggesting the involvement of magnesium ions in the hydrolysis of pyrophosphate by rat osseous plate alkaline phosphatase is proposed. (C) 1998 Published by Elsevier B.V. Ltd. All rights reserved.
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Cells from rat bone marrow exhibit the proliferation-differentiation sequence of osteoblasts, form mineralized extracellular matrix in vitro and release alkaline phosphatase into the medium. Membrane-bound alkaline phosphatase was obtained by method that is easy to reproduce, simpler and fast when compared with the method used to obtain the enzyme from rat osseous plate. The membrane-bound alkaline phosphatase from cultures of rat bone marrow cells has a MWr of about 120 kDa and specific PNPP activity of 1200 U/tng. The ecto-enzyme is anchored to the plasma membrane by the GPI anchor and can be released by PIPLC (selective treatment) or polidocanol (0.2 mg/mL protein and 1% (w/v) detergent). The apparent optimum pH for PNPP hydrolysis by the enzyme was pH 10. This fraction hydrolyzes ATP (240 U/mg), ADP (350 U/ mg), glucose 1-phosphate (1100 U/mg), glucose 6-phosphate (340 Wing), fructose 6-phosphate (460 U/mg), pyrophosphate (330 U/mg) and (3glycerophosphate (600 U/mg). Cooperative effects were observed for the hydrolysis of PPi and beta-glycerophosphate. PNPPase activity was inhibited by 0.1 mM vanadate (46%), 0.1 mM ZnCl2 (68%), 1 mM levamisole (66%), 1 mM arsenate (44%), 10 mM phosphate (21%) and 1 mM theophylline (72%). We report the biochemical characterization of membrane-bound alkaline phosphatase obtained from rat bone marrow cells cultures, using a method that is simple, rapid and easy to reproduce. Its properties are compared with those of rat osseous plate enzyme and revealed that the alkaline phosphatase obtained has some kinetics and structural behaviors with higher levels of enzymatic activity, facilitating the comprehension of the mineralization process and its function. (c) 2006 Elsevier B.V. All rights reserved.
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Purified membrane-bound alkaline phosphatase from rat osseous plate hydrolyzed pyrophosphate in the presence of magnesium ions, with a specific activity of 92.7 U/mg. Optimal apparent pH for pyrophosphatase activity was 8.0 and it remained unchanged on increasing the pyrophosphate concentration. In the absence of magnesium ions the enzyme had a K-m = 88 mu M and V = 36.7 U/mg for pyrophosphate and no inhibition by excess substrate was observed. Pyrophosphatase activity was rapidly destroyed at temperatures above 40 degrees C, but magnesium ions apparently protected the enzyme against danaturation. Sodium metavanadate (Ki = 1.0 mM) was a competitive inhibitor of pyrophosphatase activity, while levamisole (Ki = 8.2 mM) and theophylline (Ki = 7.4 mM) were uncompetitive inhibitors. Magnesium ions (K-0.5 = 1.7 mu M) stimulated pyrophosphatase activity, while cobalt (Ki = 48.5 mu M) and zinc (Ki = 22.0 mu M) ions were non-competitive inhibitors. Manganese and calcium ions had no effect on pyrophosphatase activity. The M-w of the pyrophosphatase: protein was 130 kDa by gel filtration, but a value of 65 kDa was obtained by dissociative gel electrophoresis, suggesting that it was a dimer of apparently identical subunits. These results suggested that pyrophosphatase activity stems from the membrane-bound osseous plate alkaline phosphatase and not from a different protein.
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Alkaline phosphatase is required for the mineralization of bone and cartilage. This enzyme is localized in the matrix vesicle, which plays a role key in calcifying cartilage. In this paper. we standardize a method for construction an alkaline phosphatase liposome system to mimic matrix vesicles and examine a some kinetic behavior of the incorporated enzyme. Polidocanol-solubilized alkaline phosphatase, free of detergent, was incorporated into liposomes constituted from dimyristoylphosphatidylcholine (DMPC), dilaurilphosphatidylcholine (DLPC) or dipalmitoylphosphatidylcholine (DPPC). This process was time-dependent and >95% of the enzyme was incorporated into the liposome after 4 h of incubation at 25 degreesC. Although, incorporation was more rapid when vesicles constituted from DPPC were used, the incorporation was more efficient using vesicles constituted from DMPC. The 395 nm diameter of the alkaline phosphatase-liposome system was relatively homogeneous and more stable when stored at 4 degreesC.Alkaline phosphatase was completely released from liposome system only using purified phosphatidylinositol-specific phospholipase C (PIPLC). These experiments confirm that the interaction between alkaline phosphatase and lipid bilayer of liposome is via GPI anchor of the enzyme, alone. An important point shown is that an enzyme bound to liposome does not lose the ability to hydrolyze ATP, pyrophosphate and p-nitrophenyl phosphate (PNPP), but a liposome environment affects its kinetic properties, specifically for pyrophosphate.The standardization of such system allows the study of the effect of phospholipids and the enzyme in in vitro and in vivo mineralization, since it reproduces many essential features of the matrix vesicle. (C) 2002 Elsevier B.V. Ltd. All rights reserved.
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Alkaline phosphatase is required for the mineralization of bone and cartilage. This enzyme is localized in the matrix vesicle, which plays a role key in calcifying cartilage. In this paper we standardize a method to construction a resealed ghost cell-alkaline phosphatase system to mimic matrix vesicles and examine the kinetic behavior of the incorporated enzyme. Polidocanol-solubilized alkaline phosphatase, free of detergent, was incorporated into resealed ghost cells. This process was time-dependent and practically 50% of the enzyme was incorporated into the vesicles in 40 h of incubation, at 25 degreesC. Alkaline phosphatase-ghost cell systems were relatively homogeneous with diameters of about 300 nm and were more stable when stored at -20 degreesC.Alkaline phosphatase was completely released from the resealed ghost cell-system using only phospholipase C. These experiments confirm that the interaction between alkaline phosphatase and the lipid bilayer of resealed ghost cell is exclusively via glycosylphosphatidylinositol (GPI) anchor of the enzyme.An important point shown is that an enzyme bound to resealed ghost cell does not lose the ability to hydrolyze ATP, pyrophosphate and p-nitrophenyl phosphate (PNPP), but the presence of a ghost membrane, as a support of the enzyme, affects its kinetic properties. Moreover, calcium ions stimulate and phosphate ions inhibit the PNPPase activity of alkaline phosphatase present in resealed ghost cells. (C) 2002 Elsevier B.V. B.V. All rights reserved.