Lipolytic Esterases in Staphylococci

Staphylococci split a wide range of lipid substrates by production of an enzyme complex with two main components (i) a lipase acting optimally on fat-soluble glycerides, and (ii) an esterase acting optimally on water-soluble esters. The action is dependent upon carbon chain length, interfacial dispersion, solubility, and pH of substrate and end products. The esterase is less susceptible to organophosphorus inhibitors than mammalian esterases. There is no apparent correlation between lipolysis and markers of pathogenicity such as production of coagulase and toxin, but the possession of a flexible lipolytic mechanism might account for the persistence of staphylococci in the fatty secretions of mammalian skin.     

Rates of Dissolution of Tolbutamide Tablets

An investigation was made of the pharmaceutical properties and the in vitro dissolution rates of 18 commercially available brands of tolbutamide tablets, all of which met the limits set by the Food and Drug Regulations for tablets sold in Canada.A marked variation in dissolution rates was found, which bore no relation to the official disintegration time. These wide variations in dissolution rate point to a need for (a) a comprehensive study of the in vivo effects of different tolbutamide tablets, and (b) an official test that sets limits for the rate of dissolution of tolbutamide tablets, in addition to the one that places limits on disintegration time.     

The Development of Infection Structures of Sderotium cepivorum on Onion

Growth of Sderotium cepivorum mycelium on root tissue differed from that on stem tissue. Hyphae grew along the lines of the longitudinal epidermal cell walls often producing side branches which resulted in a distinctive pattern of growth. Penetration occurred mainly between anticlinal wall junctions with occasional direct penetration through the periclinal wall. Growth on the surface of the stem resulted in the formatíon of donne shaped infection cushions, arising from repeated dichotomous branching of hyphal tips. Penetration of the stem tissue occurred solely from these structures. The results of experiments using artificial membranes and surface replicas indicated that the stimulus for attempted penetration was chemical in nature but that the nature of the infection structure produced was determined by the relative strength of the tissue under attack.     

Experimental and theoretical kinetics study of antibacterial killing mediated by human natural killer cells

We have recently shown that purified human NK cells, both resting and activated, efficiently kill gram-negative and gram-positive bacteria in vitro. To investigate the mechanism of NK cell-mediated cytotoxicity against Escherichia coli we have developed a mathematical model of the kinetics using the experimental data. The kinetics of killing are characterized by initial target bacterial multiplication, followed by rapid bacterial death. Experiments demonstrates that for each donor there is a threshold number of effector cells necessary to observe a net killing effect. Below the threshold, even use of high effector-to-target ratios lack killing activity and the bacterial growth cannot be stopped. In contrast, if the number of NK cells is larger than the threshold, complete killing is achieved, even at ratios as low as 1/1000. The threshold number varies among donors, ranging between 1200 and 12000 purified NK cells/tube, and provides a quantitative measure of antibacterial activity. Performing the assay at 4 degrees C raised the threshold number required for killing. Experiments performed in Boyden chambers confirm that NK cell-bacteria contact is not necessary for efficient killing, although the kinetics of bacterial lysis is slower. The fit between model and data supports the hypothesis that the bactericidal mechanism is extracellular and is mediated by an anti-microbial factor released from NK cells. Accumulated evidence also indicates that this factor is distinguishable from the mechanisms mediating tumor cell cytotoxicity.     

Synergistic effects of ethanol and temperature on yeast mitochondria

At temperatures lower than 37°C, the ethanol inhibition constant (Ki) for growth or fermentation inrho ⁺ cells of theSaccharomyces cerevisiae strain S288C was always higher (1.1M) than inrho ^– mutants (0.7M). At 37°C these differences disappeared, and both strains were equally inhibited by ethanol (Ki=0.7m). Mitochondrial activity can be inhibited by high ethanol concentration and temperature. In fact, the stronger inhibition by ethanol of therho ⁺ strain at 37°C was due to the fact that, under these conditions, this strain loses the advantage conferred by mitochondrial activity since the induction ofrho ^– cells in the population is very high. This does not result in an increase in the frequency ofrho ^– mutants because of the poor viability of these mutants in conditions of high temperature and ethanol. In consequence, S288C strain becomes as strongly inhibited by ethanol as therho ^– mutant strains. Differences in viability were not related to the fatty acids and ergosterol composition of the strain. In the presence of ethanol, bothrho ⁺ andrho ^– strains modified their lipids in the same way, but these changes did not improve their ethanol tolerance. They were not due to differences in adaptation to ethanol either, since after successive transfers in ethanol, growth () and fermentation () rates in therho ^– mutants were increasingly inhibited with time, whereas in the S288C strain inhibition of and by ethanol remained unaltered. Rather,rho ^– mutants are less viable thanrho ⁺ cells because of the inability of the former to respire. At 37°C the Ki increased to 0.9M ethanol either when mitochondrial from highly ethanol-tolerant wine yeasts were transferred torho ^– mutants of the strain S288C or when the mitochondria of strain S288C were preadapted by growing the strain in glycerol instead of glucose before it was cultivated in ethanol.     

Structure of genes narL and narX of the nar (nitrate reductase) locus in Escherichia coli K-12

narL and narX mediate nitrate induction of nitrate reductase synthesis and nitrate repression of fumarate reductase synthesis. We report here the nucleotide sequences of narL and narX. The deduced protein sequences aid in defining distinct subclasses of regulators and sensors in the family of two-component regulatory proteins.     

Localization of dynorphin-induced neurotoxicity in rat spinal cord

Intrathecally injected dynorphin A (1-13) in rats results in a reversible hindlimb paralysis and an irreversible loss of the tail-flick reflex. Histologic examination of the spinal cords of dynorphin treated rats demonstrated dead and/or dying neurons predominately localized in the central area which approximates Rexed lamina VII and X. In this area a maximum effect of the dynorphin-induced neurotoxicity is evident. Thus, the dynorphin-induced neuron death is suggestive of an anatomical selectivity.