Eusébio de Queirós: chefe de polícia da Corte (1833-1844)

Nesta dissertação apresentamos uma análise da trajetória de Eusébio de Queirós no período em que ele ocupava o cargo de chefe de polícia da Corte (1833-1844), momento de grande turbulência social no Império, e consolidação das posições do Regresso Conservador. Mostramos como Eusébio de Queirós se precipitou sobre o "vazio" de atribuições que caracterizava a função de chefe de polícia, tornando-se um articulador da administração da justiça na Corte, após assumir a direção de uma Secretaria de Polícia da Corte com uma estrutura precária, em meio às discussões acerca do regime policial estabelecido com a adoção do Código de Processo Criminal de 1832. A ideia de que no compartilhamento da informação entre as autoridades estava a pedra angular da segurança pública foi uma constante na trajetória de Queirós, exemplificados na abordagem dada à Revolta dos Malês (1835) e às Revoltas Liberais de 1842. Esta pesquisa trabalha uma entre as possíveis caracterizações de Eusébio de Queirós, considerando as implicações de ordens biográfica e historiográfica, procurando problematizar por meio de uma trajetória específica aspectos que circundam o processo de construção do Estado nacional no Brasil.

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An ingenious new CMOS-compatible process which promises to significantly improve the performance of power devices is discussed. A novel power device concept based on the use of high voltage regions suspended on thin semiconductor/dielectric membranes is reported. The membrane power devices are manufactured in a fully-CMOS compatible silicon-on-insulator (SOI) process followed by a bulk etching step and subsequent back-passivation. The concept is applicable to a class of high voltage devices such as LDMOSFETs, diodes, LIGBTs and superjunctions.

ISOLATION AND PROPERTIES OF A BLOOD-COAGULATION FACTOR-X ACTIVATOR FROM THE VENOM OF KING COBRA (OPHIOPHAGUS HANNAH)

A specific blood coagulation factor X activator was purified from the venom of Ophiophagus hannah by gel filtration and two steps of FPLC Mono-Q column ion-exchange chromatography. It showed a single protein band both in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and alkaline polyacrylamide gel electrophoresis. The mol. wt was estimated to be 62,000 in non-reducing conditions and 64,500 in reducing conditions by SDS-PAGE. The isoelectric point was found to be pH 5.6. The enzyme had weak amidolytic activities toward CBS 65-25, but it showed no activities on S-2266, S-2302, thrombin substrate S-2238, plasmin substrate S-2251 or factor Xa substrate S-2222. It had no arginine esterase activity toward substrate benzoylarginine ethylester (BAEE). The enzyme activated factor X in vitro and the effect was absolutely Ca2+ dependent, with a Hill coefficient of 6.83. It could not activate prothrombin nor had any effect on fibrinogen and thus appeared to act specifically on factor X. The procoagulant activity of the enzyme was almost completely inhibited by serine protease inhibitors like PMSF, TPCK and soybean trypsin inhibitor; partially inhibited by L-cysteine. Metal chelator EDTA did not inhibit its procoagulant activity. These results suggest that the factor X activator from O. hannah venom is a serine protease.