Modeling of Single-Step and Multistep Adsorption Isotherms of Organic Pesticides on Soil

2002 ◽  
Vol 50 (25) ◽  
pp. 7326-7331 ◽  
Author(s):  
Lívia N. Konda ◽  
Imre Czinkota ◽  
György Füleky ◽  
György Morovján
2015 ◽  
Vol 72 (9) ◽  
pp. 1594-1600 ◽  
Author(s):  
Azhagapillai Prabhu ◽  
Ahmed Al Shoaibi ◽  
C. Srinivasakannan

The work reports a facile synthesis procedure for preparation of porous sulfonated carbons and its suitability for adsorption of phenol. The sulfonated carbon was synthesized utilizing a simplified, single-step, shorter duration process by sulfonation, dehydration and carbonization of sucrose in sulfuric acid and tetraethylorthosilicate. The surface and internal structures of the adsorbents were characterized utilizing various characterization techniques to understand the porous nature and surface functional groups of the porous matrix. Adsorption capacity was found to be highest for the sample heat treated at 600 °C, with the maximum adsorption capacity of 440 mg/g at 30 °C. The adsorption isotherms were tested with the Freundlich and Langmuir adsorption isotherms models to identify the appropriate adsorption mechanism.


Author(s):  
Elsie M. B. Sorensen

The detoxification capacity of the liver is well documented for a variety of substances including ethanol, organic pesticides, drugs, and metals. The piscean liver, although less enzymatically active than the mammalian counterpart (1), contains endoplasmic reticulum with an impressive repertoire of oxidizing, reducing, and conjugating abilities (2). Histopathologic changes are kncwn to occur in fish hepatocytes following in vivo exposure to arsenic (3); however, ultrastructural changes have not been reported. This study involved the morphometric analysis of intracellular changes in fish parynchymal hepatocytes and correlation with arsenic concentration in the liver.Green sunfish (Lepomis cyanellus, R.) were exposed to 0, 30, or 60 ppm arsenic (as sodium arsenate) at 20°C for 1, 2, or 3 week intervals before removal of livers for quantification of the arsenic burden (using neutron activation analysis) and morphometric analysis of ultrastructural alterations. Livers were cut into 1 mm cubes for fixation, dehydration, and embedding.


2005 ◽  
Vol 173 (4S) ◽  
pp. 240-240
Author(s):  
Premal J. Desai ◽  
David A. Hadley ◽  
Lincoln J. Maynes ◽  
D. Duane Baldwin

1996 ◽  
Vol 75 (03) ◽  
pp. 497-502 ◽  
Author(s):  
Hadewijch L M Pekelharing ◽  
Henne A Kleinveld ◽  
Pieter F C.C.M Duif ◽  
Bonno N Bouma ◽  
Herman J M van Rijn

SummaryLp(a) is an LDL-like lipoprotein plus an additional apolipoprotein apo(a). Based on the structural homology of apo(a) with plasminogen, it is hypothesized that Lp(a) interferes with fibrinolysis. Extracellular matrix (ECM) produced by human umbilical vein endothelial cells was used to study the effect of Lp(a) and LDL on plasminogen binding and activation. Both lipoproteins were isolated from the same plasma in a single step. Plasminogen bound to ECM via its lysine binding sites. Lp(a) as well as LDL were capable of competing with plasminogen binding. The degree of inhibition was dependent on the lipoprotein donor as well as the ECM donor. When Lp(a) and LDL obtained from one donor were compared, Lp(a) was always a much more potent competitor. The effect of both lipoproteins on plasminogen binding was reflected in their effect on plasminogen activation. It is speculated that Lp(a) interacts with ECM via its LDL-like lipoprotein moiety as well as via its apo(a) moiety.


1983 ◽  
Vol 49 (01) ◽  
pp. 024-027 ◽  
Author(s):  
David Vetterlein ◽  
Gary J Calton

SummaryThe preparation of a monoclonal antibody (MAB) against high molecular weight (HMW) urokinase light chain (20,000 Mr) is described. This MAB was immobilized and the resulting immunosorbent was used to isolate urokinase starting with an impure commercial preparation, fresh urine, spent tissue culture media, or E. coli broth without preliminary dialysis or concentration steps. Monospecific antibodies appear to provide a rapid single step method of purifying urokinase, in high yield, from a variety of biological fluids.


1981 ◽  
Vol 31 (1) ◽  
pp. 597-601 ◽  
Author(s):  
Karim Farag ◽  
Francis Perineau ◽  
Antoine Gaset ◽  
Jacques Molinier

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