Study of ceramics from Brazilian slave quarters of the XVIII and XIX centuries by EDXRF and multivariate analysis.

This study refers to the archaeometric analysis of ceramic fragments found in archaeological excavations around slave quarters of Colégio dos Jesuítas and São Bento plantations, both located in Campos dos Goytacazes - RJ. The question whether handmade ceramics were produced by the slaves themselves or acquired through local trade networks is an open and important question in the African diaspora. Samples of clay sources and the ceramic fragments, were analyzed using the EDXRF technique with the aid of multivariate statistical analysis.

[The archeology of slavery on Jesuit fazendas: first research notes].

These preliminary research notes present theoretical and methodological questions regarding a recently inaugurated investigation in historical archeology that intends to analyze daily life under slavery, demographic regimes, cultural practices, and so on. A survey of archeological sites on former 'senzalas' (slave quarters) and slave-owning fazendas in the Paraíba Valley and northern part of the state of Rio de Janeiro is currently in progress. With the cooperation of historians, archeologists, and anthropologists, records of the material culture of slave populations, which originally comprised indigenes and later Africans, are being located at excavations underway on the fazenda that is part of the Jesuit school in Campos dos Goytacazes, Rio de Janeiro, first run by the clergy and later by members of the laity in the seventeenth, eighteenth, and nineteenth centuries.

Lactosylceramide molecular species specificity of rat liver CMP-N-acetylneuraminate:lactosylceramide sialyltransferase.

Six naturally occurring and three synthetic molecular species of lactosylceramide (LacCer) were used to examine the molecular species specificity of CMP-N-acetylneuraminate:lactosylceramide alpha 2,3-sialyltransferase in a Golgi-rich fraction of rat liver. The enzyme molecular species specificity was determined either in the presence of nonspecific lipid transfer protein or in the presence of detergents. Assays performed in the presence of transfer protein showed that for those lactosylceramide molecular species with either d18:1 or d18:0 long chain base the enzyme activity decreased linearly as the effective carbon number of the fatty acid increased.

Nonspecific lipid transfer protein in the assay of a membrane-bound enzyme CMP-N-acetyl-neuraminate:lactosylceramide sialyltransferase.

CMP-N-acetylneuraminate:lactosylceramide alpha-2,3-sialyltransferase is tightly associated with the luminal side of the Golgi membrane as is its lipid substrate, lactosylceramide. In order to understand the kinetics, properties, and regulation of this enzyme, it is necessary to alter the amount and type of substrate in the membrane while minimizing changes in the membrane environment or in the conformation of the enzyme. Therefore, nonspecific lipid transfer protein, which accelerates the transfer of phospholipids, cholesterol, and glycosphingolipids between membranes was used to study the properties and kinetics of rat liver CMP-N-acetylneuraminate:lactosylceramide sialyltransferase.