Lithium iron phosphate (LiFePO4) as an effective activator for degradation of organic dyes in water in the presence of persulfate

LiFePO4 was synthesized and successfully applied for activation of persulfate to produce sulfate radicals for dye degradation.

Cyclic ADP-ribose and related compounds activate sheep skeletal sarcoplasmic reticulum Ca2+ release channel

It has been suggested that adenosine 5'-cyclic-diphosphoribose (cADPR) can activate only nonskeletal isoforms of the ryanodine-sensitive Ca2+ release channel. We now demonstrate that cADPR is an effective activator of sheep skeletal sarcoplasmic reticulum (SR) Ca2+ release channels incorporated into planar phospholipid bilayers in the presence of activating levels of cytosolic Ca2+. In addition, the precursor of cADPR, beta-NAD+, and the metabolite, adenosine diphosphoribose (ADP-ribose), also increase the open probability (Po) of skeletal SR Ca2+ release channels in micromolar concentrations. At low concentrations of cADPR (1 microM), the mechanism for the increase in Po is an increase in the frequency of channel openings with no increase in the duration of the open events. We also show that the effect of cADPR is dependent on luminal [Ca2+]. cADPR has no effect on Po when the luminal [Ca2+] is < 40 microM. However, at millimolar concentrations of luminal Ca2+, cADPR 1 and 10 microM) increases Po in the presence of activating cytosolic Ca2+.

A New Method for the Determination of Plasma Activators of Fibrinolysis

SummaryThe term “effective activator” of plasminogen is proposed, to denote the resultant of activator-antiactivator interaction, and a method for the determination of the level of these activators is described. By adding axcess plasminogen to the euglobulin fraction of plasma the influence of the level of endogenous plasminogen and of the antiplasmin is eliminated. It is shown that the level of fibrinogen has very little bearing on the results. An effective activator unit is defined as equal to 1 CTA unit of urokinase activity on a fibrinogen-plasminogen substrate.

Charakterisierung von Staphylokokken-Nuclease / Characterization of Staphylococcus Nuclease

Two serologically different nucleases of Staphylococcus aureus were examined. One of these nucleases, the h-Nu, was from S. aureus of human origin, the other, c-Nu, from S. aureus of canine origin.Both nucleases had a pH optimum of 10.0—10.2 and needed Ca2⊕ for activation. Cu2® was also an effective activator, particularly for c-Nu. Sr2⊕ showed only little activation. Citrate stimulated the activity of h-Nu and inhibited that of c-Nu. Polyvinylsulfate inhibited both nucleases. After heating at 100°C for 2 min. both nucleases (at 0.1 mg enzyme/ml), c-Nu lost 90% and h-Nu 40% of the activity. Both nucleases also split RNA and degraded heat-denatured DNA more rapidly than native DNA.

Tetramethylthiuram Disulfide Vulcanization of Extracted Rubber. I. Introduction and Compounding

(1) Large dosages of TMTM inhibit TMTD vulcanization or vulcanization with sulfur. (2) The desirability of up to about 1.5 phr zinc oxide for TMTD vulcanization was confirmed. If an unusually large amount of TMTD (10 phr) is used, a well vulcanized stock may be obtained without zinc activation. (3) Palmitic acid displays only a mild activating effect on TMTD vulcanization. (4) Zinc dimethyldithiocarbamate, a main product of TMTD vulcanization, is not an activator for a TMTD-zinc oxide recipe. (5) Dimethylammonium dimethyldithiocarbamate does not activate TMTD-zinc oxide formulations. (6) Zinc sulfide is an effective activator for TMTD vulcanization.