Pierre Bourdieu as a Sociologist of the Economy and Critic of 'Globalisation'

This article examines Pierre Bourdieu's sociology of the economy and his more recent politically engaged interventions on 'globalisation'. Many scholars regard these as not being in the same academic league as his classic studies on taste, academia, and state elites, etc., and, instead, dismiss them as a private matter or even, as the spleen of Pierre Bourdieu, the individual. This paper questions this disjunction of the 'academic' and 'politically engaged' sides of Pierre Bourdieu's work. First, it argues that his most recent interventions against a neo-liberal globalisation were the logical result of a particular definition of intellectual practice that had been outlined before in his sociology of the intellectual field. It then demonstrates that Bourdieu's economic sociology and critique of contemporary capitalism not only does not contradict his earlier research, but that it provides valuable and original insights into the current transformation of the political economy of the advanced capitalist countries. The paper concludes with a suggestion of how to strengthen the theoretical foundation of Bourdieu's analysis of contemporary capitalism by relating it to and making it compatible with alternative approaches in the tradition of critical political economy.

The complex array of bradykinin-related peptides (BRPs) in the peptidome of pickerel frog (Rana palustris) skin secretion is the product of transcriptional economy.

Previous peptidomic analyses of the defensive skin secretion from the North American pickerel frog, Rana palustris, have established the presence of canonical bradykinin and multiple bradykinin-related peptides (BRPs). As a consequence of the multiplicity of peptides identified and their diverse primary structures, it was speculated that they must represent the products of expression of multiple genes. Here, we present unequivocal evidence that the majority of BRPs (11/13) identified in skin secretion by the peptidomic approach can be generated by differential site-specific protease cleavage from a single common precursor of 321 amino acid residues, named skin kininogen 1, whose primary structure was deduced from cloned skin secretion-derived cDNA. The organization of skin kininogen 1 consists of a hydrophobic signal peptide followed by eight non-identical domains each encoding a single copy of either canonical bradykinin or a BRP. Two additional splice variants, encoding precursors of 233 (skin kininogen 2) or 189 amino acid residues (skin kininogen 3), were also cloned and were found to lack BRP-encoding domains 5 and 6 or 4, 5 and 6, respectively. Thus, generation of peptidome diversity in amphibian defensive skin secretions can be achieved in part by differential protease cleavage of relatively large and multiple-encoding domain precursors reflecting a high degree of transcriptional economy.

Energetics and water economy of common spiny mice Acomys cahirinus from north- and south-facing slopes of a Mediterranean valley

1. A comparison was made of the daily energy expenditure (DEE), resting metabolic rate (RMR) and water turnover (WTO) of two populations of Common Spiny Mice Acomys cahirinus from north- and south-facing slopes (NFS and SFS) of the same valley, which represented 'Mediterranean' and 'desert' habitats, respectively.