Transbilayer distribution of bromine in fluid bilayers containing a specifically brominated analogue of dioleoylphosphatidylcholine

We describe in this paper the transbilayer distribution of the bromines of the specifically halogenated phospholipid 1-oleoyl-2-(9,10-dibromostearoyl)-sn-glycero-3- phosphocholine (OBPC). The distribution was determined by X-ray diffraction of oriented multilayers of mixtures of OBPC and 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) at 66% relative humidity by the general approach of Franks et al. (1978) [Nature 276, 530-532]. The bromine distribution of OBPC in the fluid L alpha phase is described accurately by a pair of Gaussian functions located 7.97 +/- 0.27 A from the center of the bilayer with l/e half-widths of 4.96 +/- 0.62 A. We find that OBPC bilayers are accurately described as DOPC bilayers with an additional bromine distribution centered at the position of the double bond of DOPC and conclude that OBPC is an excellent structural isomorph for DOPC under the conditions of these experiments. The distribution obtained is the complete and fully resolved transbilayer image of the halogen label because the broad distribution of the bromines is due entirely to thermal disorder and not to experimental limitations [Wiener, M. C., & White, S. H. (1991a) Biophys. J. 59, 162-173]. The observed width of the bromine distribution indicates that virtually all of the hydrocarbon interior is accessible to the bromines. The distance between the bromine/double-bond position and the headgroup phosphate position was determined from one-dimensional Patterson maps and found to be approximately 12 A. The application of accurately determined bromine distributions to the quantitative interpretation of fluorescence quenching experiments is discussed. A method for the self-consistent global analysis of diffraction data from mixtures that permits the use of data sets with different instrumental scale factors is developed in an Appendix.     

Cartography and Clandestinité in Leïla Sebbar’s Shérazade: 17 ans, brune, frisée, les yeux verts

In this paper, I read Leïla Sebbar’s staging in her novel Shérazade: 17 ans, brune, frisée, les yeux verts of the resistance by children of North African and other immigrants in the early 1980s to the French state’s cartographic modes and documents of control. The paper will consider the many uses to which the map was put by the French state in its colonization of North Africa and particularly Algeria, and later in its attempts to control the banlieues its policies of citizenship and cartographic control yielded on the margins of Paris. In this context, I will explore the ways in which the novel’s characters, living clandestinely in a squatt, simultaneously resist, put to use, and even supercede state documents of control as they disrupt everyday life and conduct heists across the city of Paris. The paper will explore unofficial cartographies of Paris, from those afforded by the radios libres and alternative publications such as Libération and Sans Frontièrez, to oral and almost proverbial networks of knowledge criss-crossing the city of Paris, while also tracing the uses to which supplemental cartographic sketches and counterfeit identity cards are put in the pages of the novel. The paper will be in dialogue with theoretical and critical formulations of space, cartography, and state control put forward by Michel de Certeau, Henri Lefebvre, Michel Foucault, and Tom Conley. The paper will conclude with a consideration of the means and limits of resistance by the novel’s characters in the context of this body of theory and criticism.     

Chicken riboflavin-binding protein. cDNA sequence and homology with milk folate-binding protein

The Rd gene is expressed in the livers and oviducts of laying hens and codes for the riboflavin-binding protein (RfBP) of egg yolk and egg white. A lambda gt11 cDNA library derived from chicken oviduct poly(A)+ RNA was screened with polyclonal rabbit antiserum to chicken RfBP. Positive clones were isolated and rescreened with a mixed oligonucleotide probe corresponding to residues 20-25 of the mature protein. The largest cDNA clone (969 base pairs) was subcloned into plasmid pIBI21, and the nucleotide sequence was determined by the dideoxynucleotide method. This clone contained the entire coding region for RfBP. The published amino acid sequence of the mature protein was confirmed. In addition, the following 17-residue signal peptide was deduced: Met-Leu-Arg-Phe-Ala-Ile-Thr-Leu-Phe-Ala-Val-Ile-Thr-Ser-Ser-Thr-Cys. Unexpectedly, the nucleotide sequence codes for 2 adjacent arginine residues at the carboxyl terminus that are not observed in the mature protein. The amino acid sequence of RfBP is homologous with bovine milk folate-binding protein. Eight of the nine pairs of cysteines involved in disulfide bonds in RfBP are conserved in folate-binding protein, as are all of the tryptophan residues. Sequence identity between homologous regions of these two vitamin-binding proteins is more than 30%.     

Cascade of autophosphorylation in the beta-subunit of the insulin receptor

Insulin stimulated autophosphorylation of the beta-subunit of the insulin receptor purified from Fao hepatoma cells or purified from Chinese hamster ovary (CHO/HIRC) or Swiss 3T3 (3T3/HIRC) cells transfected with the wild-type human insulin receptor cDNA. Autophosphorylation of the purified receptor occurred in at least two regions of the beta-subunit: the regulatory region containing Tyr-1146, Tyr-1150, and Tyr-1151, and the C-terminus containing Tyr-1316 and Tyr-1322. In the presence of antiphosphotyrosine antibody (alpha-PY), autophosphorylation of the purified receptor was inhibited nearly 80% during insulin stimulation. Tryptic peptide mapping showed that alpha-PY inhibited autophosphorylation of both tyrosyl residues in the C-terminus and one tyrosyl residue in the regulatory region, either Tyr-1150 or Tyr-1151. Thus, a bis-phosphorylated form of the regulatory region accumulated in the presence of alpha-PY, which contained Tyr(P)-1146 and either Tyr(P)-1150 or 1151. In intact Fao, CHO/HIRC, and 3T3/HIRC cells, insulin stimulated tyrosyl phosphorylation of the beta-subunit of the insulin receptor. Tryptic peptide mapping indicated that the regulatory region of the beta-subunit was mainly (greater than 80%) bis-phosphorylated; however, all three tyrosyl residues of the regulatory region were phosphorylated in about 20% of the receptors. As the phosphotransferase was activated by tris-phosphorylation but not bis-phosphorylation of the regulatory region of the beta-subunit (White et al.: Journal of Biological Chemistry 263:2969-2980, 1988), the extent of autophosphorylation in the regulatory region may play an important regulatory role during signal transmission in the intact cell.