Can the Sofa Speak? A Look at Thing Theory

Things (ed. Bill Brown) The Fugitive’s Properties: Law and the Poetics of Possession (Stephen M. Best) Photographs Objects Histories: On the Materiality of Images (ed. Elizabeth Edwards and Janice Hart) Things That Talk: Object Lessons from Art and Science (ed. Lorraine Daston

The Victorian Anthropocene: George Marsh and the Tangled Bank of Darwinian Environmentalism

There is an important  19th century  turning-point in thinking about the Anthropocene.  Vermont environmentalist George Marsh's 1864 Man and Nature: or, Physical Geography as Modified by Human Action is a seminal account of how the unintended consequences of human action give humans a previously unsuspected role to play in secular terrestrial change. The role that Darwinian 'natural materialism' played in  shaping Marsh's insights is profound, and grasping the particular developments in biological thinking that made his work feasible casts a useful side-light on our own current assumptions about humanity's relationship to the environment, and suggests some ways of thinking about which of those assumptions have the potential to shape further thought and large-scale human action.      

N‐terminus of hMLH1 confers interaction of hMutLα and hMutLβ with hMutSα

Mismatch repair is a highly conserved system that ensures replication fidelity by repairing mispairs after DNA synthesis. In humans, the two protein heterodimers hMutSα (hMSH2‐hMSH6) and hMutLα (hMLH1‐hPMS2) constitute the centre of the repair reaction. After recognising a DNA replication error, hMutSα recruits hMutLα, which then is thought to transduce the repair signal to the excision machinery. We have expressed an ATPase mutant of hMutLα as well as its individual subunits hMLH1 and hPMS2 and fragments of hMLH1, followed by examination of their interaction properties with hMutSα using a novel interaction assay. We show that, although the interaction requires ATP, hMutLα does not need to hydrolyse this nucleotide to join hMutSα on DNA, suggesting that ATP hydrolysis by hMutLα happens downstream of complex formation. The analysis of the individual subunits of hMutLα demonstrated that the hMutSα–hMutLα interaction is predominantly conferred by hMLH1. Further experiments revealed that only the N‐terminus of hMLH1 confers this interaction. In contrast, only the C‐terminus stabilised and co‐immunoprecipitated hPMS2 when both proteins were co‐expressed in 293T cells, indicating that dimerisation and stabilisation are mediated by the C‐terminal part of hMLH1. We also examined another human homologue of bacterial MutL, hMutLβ (hMLH1–hPMS1). We show that hMutLβ interacts as efficiently with hMutSα as hMutLα, and that it predominantly binds to hMutSα via hMLH1 as well

Crosslinked agarose encapsulated sorbents resistant to steam sterilization. Preparation and mechanical properties

The application of agarose in hemoperfusion is hampered by the lack of a suitable sterilization method. A technique has been developed for the crosslinking of agarose encapsulated sorbents by the reaction with 1,3-dichloro-2-propanol (DCP) under strong alkaline conditions. A twofold molar excess of DCP with respect to agarose and an equimolar amount of sodium hydroxide at a concentration of 0.3 mol/L with a reaction time of 1-4 h at 50°C are found to be the optimal conditions. The compressive strength of crosslinked beads is increased by a factor of 4. Agarose capsules are found to degrade by the influence of Y radiation, but are resistant to steam sterilization at 134°C during at least 30 min when crosslinked