Michel Foucault and Dorothy Smith in Case File Research: Strange Bedfellows or Complimentary Thinkers?

The aim of this article is to provide an exploration how the work of two theorists with notably different stances could be used effectively to enhance critical research methods in relation to the history of child welfare social work. The design and implementation of child welfare policies, practices and discourses could considerably benefit from a more historically well grounded scholarship that enables actors to connect their present concerns with the broader historical dynamics of social regulation. The article reports on how the work of Michel Foucault and Dorothy E. Smith might be considered in parallel as two different perspectives to the same scene in time and place. The differences and similarities in their approaches are explored with an emphasis on concepts most relevant to researching child welfare archives including discourse, text, the subject and power-knowledge. The article concludes with a commentary on further development to take forward this methodological analysis.

The last meal of the Late Ordovician mollusc ‘Helminthochiton’ thraivensis Reed, 1911, from the Lady Burn Starfish Beds, southwest Scotland.

An exceptional specimen of the Late Ordovician mollusc ‘Helminthochiton’ thraivensis Reed, from the Katian of the Lady Burn Starfish Beds, southwest Scotland, preserves gut contents that include nine pelmatozoan ossicles. These are interpreted as including two nodal and five intermodal columnals, and two radice ossicles from the attachment structure. The stem was cyclocyclic and heteromorphic, possibly N212. Radice ossicles were wider than the height of nodals, so radice scars must have encroached onto the latera of adjacent pluricolumnals. These features were compared with the 26 known pelmatozoan taxa from the Lady Burn Starfish Beds. Paracrinoids (one species) and glyptocystitid rhombiferans (six species) were discounted as prey because of their cemented attachment, and incorrect columnal morphology and lack of attachment, respectively. Of 19 species of crinoids, eight are discounted in which the column is pentagonal, tetragonal or unknown. Of the remaining eleven species, only the monobathrid camerate Macrostylocrinus cirrifer Ramsbottom satisfies all criteria for identification of the prey, including heteromorphy and radice scars encroaching adjacent internodals.

Subdivision of the bacterioferritin comigratory protein family of bacterial peroxiredoxins based on catalytic activity

Peroxiredoxins are ubiquitous proteins that catalyze the reduction of hydroperoxides, thus conferring resistance to oxidative stress. Using high-resolution mass spectrometry, we recently reclassified one such peroxiredoxin, bacterioferritin comigratory protein (BCP) of Escherichia coli, as an atypical 2-Cys peroxiredoxin that functions through the formation of an intramolecular disulfide bond between the active and resolving cysteine. An engineered E. coli BCP, which lacked the resolving cysteine, retained enzyme activity through a novel catalytic pathway. Unlike the active cysteine, the resolving cysteine of BCP peroxiredoxins is not conserved across all members of the family. To clarify the catalytic mechanism of native BCP enzymes that lack the resolving cysteine, we have investigated the BCP homologue of Burkholderia cenocepacia. We demonstrate that the B. cenocepacia BCP (BcBCP) homologue functions through a 1-Cys catalytic pathway. During catalysis, BcBCP can utilize thioredoxin as a reductant for the sulfenic acid intermediate. However, significantly higher peroxidase activity is observed utilizing glutathione as a resolving cysteine and glutaredoxin as a redox partner. Introduction of a resolving cysteine into BcBCP changes the activity from a 1-Cys pathway to an atypical 2-Cys pathway, analogous to the E. coli enzyme. In contrast to the native B. cenocepacia enzyme, thioredoxin is the preferred redox partner for this atypical 2-Cys variant. BCP-deficient B. cenocepacia exhibit a growth-phase-dependent hypersensitivity to oxidative killing. On the basis of sequence alignments, we believe that BcBCP described herein is representative of the major class of bacterial BCP peroxiredoxins. To our knowledge, this is the first detailed characterization of their catalytic activity. These studies support the subdivision of the BCP family of peroxiredoxins into two classes based on their catalytic activity.