Autoxidation of mono-, di-, and trilinoleoyl glycerols at different concentrations

Mono-, di-, and trilinoleoyl glycerols were diluted with 1-undecanol or hexadecane to produce specific concentrations, and their oxidation processes were measured at 65 degrees C at 12% relative humidity. The rate constants for oxidation of the linoleoyl residue were proportional to the concentration for all substrates. This fact suggests that no intramolecular radical chain reaction between the linoleoyl residues occurred.     

On the stability of the stock-harvesting system controlled by a feedback management procedure

Stability of the stock-harvesting system regulated by a feedback control procedure of catch quota is examined. In the procedure considered, catch quota is changed proportionally to the difference between current and the target stock level (with a proportionality constant h) and to the annual stock growth rate (with a proportionality constant g). Condition for the local stability of the target equilibrium is obtained as a function of the stock-recruitment relation, survival probability of adults, target stock level, time lag before implementation of regulation, age of sexual maturity of the stock, and proportionality constants g and h. It is shown that, (1) the procedure has the stabilizing effect; it can stabilize the target stock level that is unstable under constant harvest, (2) lower target stock level favors larger g and smaller h, when the target is set around MSYL (the stock level that gives MSY), (3) the degree of stability, measured by the time required to recover the target stock level, is an increasing function of the target stock level, (4) stability and sustainable yield are in trade-off, (5) time delay caused by the time needed before sexual maturity does not affect the stability significantly, but the effect of the time lag before implementation of regulation is significant. Comparison between harvest-control and effort-control procedures is also made, and the advantage of the latter in terms of stability is shown.     

Poly(ADP ribose) polymerase-defective mutant cell clone of mouse L1210 cells.

By a sequential mutation and selection utilizing N-methyl-N'-nitro-N-nitrosoguanidine as a mutagen, we succeeded in separating a poly(ADP ribose) polymerase-defective mutant clone (Cl-3527) from a mouse L1210 cell clone (Cl-3). The enzyme activity per cell in Cl-3527 cells was only 8% of that in wild type L1210 (CCL 219) cells. Immunoblot analysis of the enzyme protein in crude extracts of the mutant and wild type cells revealed that the enzyme defect was manifested as the loss of a 113-kDa wild type enzyme band in Cl-3527. Further analysis of partially purified enzyme from Cl-3527 by immunoblotting revealed that the molecular size of the enzyme in Cl-3527 was 108 kDa and that the amount of the mutant enzyme protein was markedly decreased in Cl-3527. The mutant enzyme was much more heat-labile than the wild type enzyme but the Km for NAD+, requirements for Mg2+ and nicked DNA, and the inhibition by 3-aminobenzamide, a potent inhibitor of the enzyme, however, were not so different from those of wild type enzyme. The mutant cells showed prolonged doubling time, increased temperature-sensitivity, increased percentage of active enzyme on a treatment of cells at high temperature, and increased expression of plasma membrane NADase, compared to wild type cells. Introduction of wild type ADPR pol gene into Cl-3527 cells partially restored the ADPR pol activity and the heat-resistance.     

Membrane aberrancy and unfolded proteins activate the endoplasmic reticulum stress sensor Ire1 in different ways

Eukaryotic cells activate the unfolded-protein response (UPR) upon endoplasmic reticulum (ER) stress, where the stress is assumed to be the accumulation of unfolded proteins in the ER. Consistent with previous in vitro studies of the ER-luminal domain of the mutant UPR initiator Ire1, our study show its association with a model unfolded protein in yeast cells. An Ire1 luminal domain mutation that compromises Ire1's unfolded-protein-associating ability weakens its ability to respond to stress stimuli, likely resulting in the accumulation of unfolded proteins in the ER. In contrast, this mutant was activated like wild-type Ire1 by depletion of the membrane lipid component inositol or by deletion of genes involved in lipid homeostasis. Another Ire1 mutant lacking the authentic luminal domain was up-regulated by inositol depletion as strongly as wild-type Ire1. We therefore conclude that the cytosolic (or transmembrane) domain of Ire1 senses membrane aberrancy, while, as proposed previously, unfolded proteins accumulating in the ER interact with and activate Ire1.     

Uncomfortable and unpleasant sensations in the legs without an urge to move as the initial manifestation of Parkinson’s disease

Sleep and Biological Rhythms - A 74-year-old man presented with creepy, dull and restless sensation of the legs for a year. The abnormal leg sensation occurred predominantly during rest and...