Why Doesn't the Creed Read "Always Be Critical"? An Examination of a Liberal Curriculum

Using ethnographic data collected in a second grade classroom over the course of a school year, this paper describes the ways in which one school's discourse of liberalism is deleteriously deployed. We view the school's discipline creed as emblematic of the school's liberal curriculum, and interrogate the effects on four African American boys in the classroom when the school enacts this creed. Despite the agency that these boys obviously had, they were unable to control the ways in which they were placed at a structural disadvantage and manipulated by a system far more powerful than they were. The results were that these four boys suffered. Not only did the intended liberal curriculum fail to be translated fully into the enacted curriculum, the liberal underpinnings of this curriculum precluded teachers and students from taking any critical stance.     

Neurotrophic control of the transmembrane Cl− pump in mammalian muscle fibers

Resting membrane potential of both innervated and denervated rat diaphragm muscle fibers was investigated when the concentration of potential-producing ions was changed in the external fluid and following treatment with furosemide. It was found that equilibrium potential ( ) equalled resting potential level in innervated muscle for Cl^–, but shifts to more positive values compared with resting membrane potential following section of the nerve. Furosemide retards development of post-denervation depolarization of the muscle membrane. It is deduced that trophic influences originating from the motor nerve activates the furosemide-sensitive Cl^– influx system, leading to raised intracellular concentration of Cl^–, a shift in (E_Cl) and depolarization of the muscle membrane.S. V. Kurashov Medical Institute, Minsitry of Health of the RSFSR, Kazan'. Translated from Neirofiziologiya, Vol. 19, No. 6, pp. 766–771, November–December, 1987.     

Components of human complement system. Testing and isolation of C3 and C5

Modified reagents for testing the hemolytic activity of human complement components, C3 and C5, have been obtained. These reagents were obtained by treatment of human blood serum pools with a saturated solution of KBr (reagent R3) or 2 M KSCN and denaturated yeasts (reagent R5). These reagents were found to be rich in the serum factor obtained through the use of DEAE-cellulose DE-52 and containing the active component of the complement (C4). To test the sensitivity and specificity of the above reagents, components C3 and C5 were purified. After this procedure these components emerged as hemolytically active, electrophoretically and immunophoretically homogeneous components, C3 and C5. DEAE-cellulose DE-52, DEAE-Sephacel, Hydroxylapatite and Ultra-gel AcA-34 were used consecutively as purification agents. The activity yields of components C3 and C5 with regard to the initial serum levels were 31% and 18%, respectively.     

The central role of protein S12 in organizing the structure of the decoding site of the ribosome

The ribosome decodes mRNA by monitoring the geometry of codon–anticodon base-pairing using a set of universally conserved 16S rRNA nucleotides within the conformationally dynamic decoding site. By applying single-molecule FRET and X-ray crystallography, we have determined that conditional-lethal, streptomycin-dependence mutations in ribosomal protein S12 interfere with tRNA selection by allowing conformational distortions of the decoding site that impair GTPase activation of EF-Tu during the tRNA selection process. Distortions in the decoding site are reversed by streptomycin or by a second-site suppressor mutation in 16S rRNA. These observations encourage a refinement of the current model for decoding, wherein ribosomal protein S12 and the decoding site collaborate to optimize codon recognition and substrate discrimination during the early stages of the tRNA selection process.