The Role of Historical Narrative in Biblical Thought:the Tendencies Underlying Old Testament Historiography

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/68403/2/10.1177_030908928100602102.pd

The Effect of Isopropyl Alcohol and Non-Ionic Surfactant Mixtures on the Wetting of Porous Coated Paper

The influence of isopropyl alcohol and non-ionic surfactant solutions on aqueous droplet wetting behaviour on porous coated paper was determined. Paper coatings provide a micro- and nano-porous surface structure, which strictly speaking cannot be described in simple roughness terms as sub-surface lateral absorption directly impacts on the apparent contact angle. It is this very deviation from an idealised system that leads to novel wetting phenomena. Isopropyl alcohol and surfactant-based systems, both of which are commonly used in the printing industry, show differences in wetting behaviour, on both short and long timescales, with changes in the relative composition of the mixtures. Small variations of 0.1 wt% in surfactant concentration have a dramatic influence on the dynamic surface tension, and thus the wetting. It was observed that the wetting kinetics for isopropyl alcohol and surfactant solutions were different in terms of both wetting area and the penetration rate, even in cases where the dynamic surface tension of the solutions was kept the same. Different stages in the wetting and following drying processes could be observed with near infrared spectral imaging. In addition, the surfactant chemistries such as their degrees of hydrophilicity and molecular weights generated comparative differences in the wetting kinetics. The dominating factor affecting the wetting was, as expected, the solid–liquid interfacial energy defined on the practical porous substrate, which differed from the direct comparison with dynamic surface tension, thus exemplifying the deviation from idealised surface roughness behaviour when considering porous materials. An apparent “equivalent” surface roughness value for the porous material was determined, and it was seen that an increase in this equivalent parameter enhanced the rate of wetting behaviour with decreasing solution surface tension, and so also affected the wetting evolution. The wetting was enhanced by cavities in the coating layer, which were enlarged by the penetrating liquids

CASP, the Alternatively Spliced Product of the Gene Encoding the CCAAT-Displacement Protein Transcription Factor, Is a Golgi Membrane Protein Related to Giantin

Large coiled-coil proteins are being found in increasing numbers on the membranes of the Golgi apparatus and have been proposed to function in tethering of transport vesicles and in the organization of the Golgi stack. Members of one class of Golgi coiled-coil protein, comprising giantin and golgin-84, are anchored to the bilayer by a single C-terminal transmembrane domain (TMD). In this article, we report the characterization of another mammalian coiled-coil protein, CASP, that was originally identified as an alternatively spliced product of the CUTL1 gene that encodes CCAAT-displacement protein (CDP), the human homologue of the Drosophila homeodomain protein Cut. We find that the Caenorhabditis elegans homologues of CDP and CASP are also generated from a single gene. CASP lacks the DNA binding motifs of CDP and was previously reported to be a nuclear protein. Herein, we show that it is in fact a Golgi protein with a C-terminal TMD and shares with giantin and golgin-84 a conserved histidine in its TMD. However, unlike these proteins, CASP has a homologue in Saccharomyces cerevisiae, which we call COY1. Deletion of COY1 does not affect viability, but strikingly restores normal growth to cells lacking the Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptor Gos1p. The conserved histidine is necessary for Coy1p's activity in cells lacking Gos1p, suggesting that the TMD of these transmembrane Golgi coiled-coil proteins is directly involved in their function