21 research outputs found

    A study on the thermal degradation of rubber in dilute solutions

    No full text
    The kinetics of low-temperature (60-100°C.) thermal degradation of deproteinized and deresinified petroleum ether soluble fraction of natural rubber in two chemically inert solvents, cyclohexane and trans-decalin, have been studied. The changes in Mw, A2, and (r-2-)½at various stages of degradation have been obtained from the lightscattering data. The rate constants and the energy of activation for chain scission have been calculated from the observed variation in Mu. The scission has been found to be random and the average energy of activation is 25.8 kcal./mole. This low-energy requirement suggests the presence of weak links in the rubber molecule which get ruptured at low temperature

    Knockout of GARPs and the β-subunit of the rod cGMP-gated channel disrupts disk morphogenesis and rod outer segment structural integrity

    No full text
    Ion flow into the rod photoreceptor outer segment (ROS) is regulated by a member of the cyclic-nucleotide-gated cation-channel family; this channel consists of two subunit types, α and β. In the rod cells, the Cngb1 locus encodes the channel β-subunit and two related glutamic-acid-rich proteins (GARPs). Despite intensive research, it is still unclear why the β-subunit and GARPs are coexpressed and what function these proteins serve. We hypothesized a role for the proteins in the maintenance of ROS structural integrity. To test this hypothesis, we created a Cngb1 5′-knockout photoreceptor null (Cngb1-X1). Morphologically, ROSs were shorter and, in most rods that were examined, some disks were misaligned, misshapen and abnormally elongated at periods when stratification was still apparent and degeneration was limited. Additionally, a marked reduction in the level of channel α-subunit, guanylate cyclase I (GC1) and ATP-binding cassette transporter (ABCA4) was observed without affecting levels of other ROS proteins, consistent with a requirement for the β-subunit in channel assembly or targeting of select proteins to ROS. Remarkably, phototransduction still occurred when only trace levels of homomeric α-subunit channels were present, although rod sensitivity and response amplitude were both substantially reduced. Our results demonstrate that the β-subunit and GARPs are necessary not only to maintain ROS structural integrity but also for normal disk morphogenesis, and that the β-subunit is required for normal light sensitivity of the rods
    corecore