Movements of Phosphorus Between its Biologically Important Forms in Lake Water

1973 ◽  
Vol 30 (10) ◽  
pp. 1525-1536 ◽  
Author(s):  
D. R. S. Lean
Keyword(s):  
Molecular Weight ◽  
Lake Water ◽  
Membrane Filtration ◽  
Organic Phosphorus ◽  
Gel Filtration ◽  
Particulate Fraction ◽  
Low Molecular Weight ◽  
Radioactive Phosphorus ◽  
Dissolved Phosphorus ◽  
Kinetics Of

A model consistent with the kinetics of phosphorus in epilimnetic lake water was developed. Adding 32PO4 to lake water and separating the major forms of dissolved phosphorus by Sephadex gel filtration showed that the exchange mechanism between inorganic phosphate and the particulate fraction predominates. At the same time, a low-molecular-weight phosphorus compound is excreted which combines with colloids in lake water, releasing phosphate from the colloid and making the phosphate available for "transfer" again. This rapid cycling of phosphorus between the four principal forms — the particulate fraction, the low-molecular-weight P compound, colloidal P, and phosphate — appears to contribute to formation of colloids in lake water. No direct complexing of phosphate to the colloid was observed. Only in the presence of algae, bacteria, and other particulate matter did the radioactive phosphorus move to the low-molecular weight and the colloidal forms. The low-molecular-weight compound is negatively charged, as is the colloidal P, but to a lesser degree. Both are removed by anion exchange materials along with phosphate, but the rate that they move into the fraction removed by membrane filtration is different from that for phosphate. When filtrate is refiltered a large amount of the colloidal P is retained by the filter. This complicates measurements of transfer and makes previous studies on utilization of dissolved organic phosphorus of doubtful value since corrections for filter retention were rarely, if ever, made.

In Vivo Studies on the Inhibition of Coagulation by Fractionated Heparin and by a Heparin Analogue I. Effects of Heparin Fractions

1981 ◽  
Vol 46 (03) ◽  
pp. 612-616 ◽  
Author(s):  
U Schmitz-Huebner ◽  
L Balleisen ◽  
F Asbeck ◽  
J van de Loo
Keyword(s):  
Molecular Weight ◽  
Day Treatment ◽  
Gel Filtration ◽  
Weight Fraction ◽  
In Vivo Studies ◽  
Low Molecular Weight ◽  
High Molecular Weight Fraction ◽  
Platelet Factor ◽  
Heparin Fractions

SummaryHigh and low molecular weight heparin fractions obtained by gel filtration chromatography of sodium mucosal heparin were injected subcutaneously into six healthy volunteers and compared with the unfractionated substance in a cross-over trial. Equal doses of 5,000 U were administered twice daily over a period of three days and heparin activity was repeatedly controlled before and 2, 4, 8 hrs after injection by means of the APTT, the anti-Xa clotting test and a chromogenic substrate assay. In addition, the in vivo effect of subcutaneously administered fractionated heparin on platelet function was examined on three of the volunteers. The results show that s.c. injections of the low molecular weight fraction induced markedly higher anti-Xa activity than injections of the other preparations. At the same time, APTT results did not significantly differ. Unfractionated heparin and the high molecular weight fraction enhanced ADP-induced platelet aggregation and collagen-mediated MDA production, while the low molecular weight fraction hardly affected these assays, but potently inhibited thrombin-induced MDA production. All heparin preparations stimulated the release of platelet Factor 4 in plasma. During the three-day treatment periods, no side-effects and no significant changes in the response to heparin injections were detected.

scholarly journals Investigating Lignin-Derived Monomers and Oligomers in Low-Molecular-Weight Fractions Separated from Depolymerized Black Liquor Retentate by Membrane Filtration

Molecules ◽  
2021 ◽  
Vol 26 (10) ◽  
pp. 2887
Author(s):  
Kena Li ◽  
Jens Prothmann ◽  
Margareta Sandahl ◽  
Sara Blomberg ◽  
Charlotta Turner ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Performance ◽  
Membrane Filtration ◽  
Black Liquor ◽  
Complex Mixture ◽  
Value Added ◽  
Kraft Pulping ◽  
Classification Model ◽  
Low Molecular Weight ◽  
Chemical Complexity

Base-catalyzed depolymerization of black liquor retentate (BLR) from the kraft pulping process, followed by ultrafiltration, has been suggested as a means of obtaining low-molecular-weight (LMW) compounds. The chemical complexity of BLR, which consists of a mixture of softwood and hardwood lignin that has undergone several kinds of treatment, leads to a complex mixture of LMW compounds, making the separation of components for the formation of value-added chemicals more difficult. Identifying the phenolic compounds in the LMW fractions obtained under different depolymerization conditions is essential for the upgrading process. In this study, a state-of-the-art nontargeted analysis method using ultra-high-performance supercritical fluid chromatography coupled to high-resolution multiple-stage tandem mass spectrometry (UHPSFC/HRMSn) combined with a Kendrick mass defect-based classification model was applied to analyze the monomers and oligomers in the LMW fractions separated from BLR samples depolymerized at 170–210 °C. The most common phenolic compound types were dimers, followed by monomers. A second round of depolymerization yielded low amounts of monomers and dimers, while a high number of trimers were formed, thought to be the result of repolymerization.

HEMODIALYSIS OF THE RAT

1966 ◽  
Vol 44 (5) ◽  
pp. 849-859 ◽  
Author(s):  
Sumner M. Robinson ◽  
David A. Hurwitz ◽  
Robert Louis-Ferdinand ◽  
William F. Blatt
Keyword(s):  
Molecular Weight ◽  
Gel Filtration ◽  
Low Molecular Weight

A technique is described for hemodialysis of either anesthetized or non-restrained rats. In the apparatus the dialysis plates of an autoanalyzer system are used with only minor modification. The efficiency of this method has been evaluated with regard to the clearance of saccharides, both in vitro and in vivo, as well as the extraction of nitrogenous low molecular weight moieties from circulating blood. Approximately 50% of the dialyzable material was obtained in a 1-hour dialysis. Further fractionation of the dialyzate was accomplished by gel filtration (Sephadex G-25).

Kinetics of the reaction of the first metabolite of fenitropan with some low molecular weight thiols

1989 ◽  
Vol 26 (3) ◽  
pp. 253-259 ◽  
Author(s):  
Gabor Gullner ◽  
Gyula Josepovits ◽  
Gyula Mikite
Keyword(s):  
Molecular Weight ◽  
Low Molecular Weight ◽  
Kinetics Of

Kinetics of inhibition of purified bovine neutrophil matrix metalloproteinase 9 by low–molecular-weight inhibitors

2009 ◽  
Vol 70 (5) ◽  
pp. 633-639 ◽  
Author(s):  
Gregory A. Bannikov ◽  
Jeffrey Lakritz ◽  
Christopher Premanandan ◽  
John S. Mattoon ◽  
Eric J. Abrahamsen
Keyword(s):  
Molecular Weight ◽  
Matrix Metalloproteinase ◽  
Matrix Metalloproteinase 9 ◽  
Low Molecular Weight ◽  
Kinetics Of ◽  
Metalloproteinase 9 ◽  
Kinetics Of Inhibition ◽  
Bovine Neutrophil

scholarly journals Role of serum IgA. Hepatobiliary transport of circulating antigen.

1981 ◽  
Vol 153 (4) ◽  
pp. 968-976 ◽  
Author(s):  
M W Russell ◽  
T A Brown ◽  
J Mestecky
Keyword(s):  
Molecular Weight ◽  
Human Serum Albumin ◽  
Gel Filtration ◽  
Low Molecular Weight ◽  
Serum Iga ◽  
Circulating Antigen ◽  
Circulating Antigens ◽  
Iga Antibody ◽  
Immune Spleen Cell

The IgA mediated hepatobiliary excretion of antigen from the circulation was studied using a radiolabeled haptenated protein (dinitrophenyl-human serum albumin) injected intravenously in mice together with monoclonal anti-dinitrophenyl antibodies of different immunoglobulin classes. Antibodies were obtained from ascitic fluids of mice bearing the MOPC315 myeloma (IgA), or immune spleen cell hybridomas (IgG and IgM). IgA antibody brought about the transport of large amounts of antigen from the circulation to the bile during 1-3h. Analysis of bile by gel filtration showed that a large part of the transported antigen remained intact and complexed with IgA. Neither IgA of different specificity nor anti-dinitrophenyl IgM medicated biliary transport of antigen. With anti-dinitrophenyl IgG, only small amounts of low molecular weight fragments of labeled antigen were found in he bile. Preformed immune complex of radiolabeled antigen and IgA antibody were rapidly transported from the circulation to the bile, resulting in threefold-higher levels of radioactivity in bile than in serum. It is proposed that an important function of serum IgA is to mediate the hepatobiliary excretion of corresponding circulating antigens.

In Vivo Studies On The Inhibition Of Coagulation By Fractionated Heparin

1981 ◽  
Author(s):  
U Schmitz-Huebner ◽  
L Balleisen ◽  
F Asbeck ◽  
J van de Loo
Keyword(s):  
Molecular Weight ◽  
Low Molecular Weight Heparin ◽  
Gel Filtration ◽  
In Vivo Studies ◽  
Low Molecular Weight ◽  
Chromogenic Substrate ◽  
Serotonin Content ◽  
Heparin Activity ◽  
Heparin Fractions

Recent investigations suggest that low molecular weight heparin may have advantages over conventional heparin with regard to the prevention of venous thrombosis and haemorrhagic side effects.High (HMW) and low (LMW) molecular weight heparin fractions with mean MWs of 16,000 and 8,800 respectively, obtained by gel filtration chromatography of sodium mucosal heparin (B. Braun Melsungen), were injected subcutaneously into six volunteers and compared with the unfractionated substance in a cross-over trial. Doses of 5,000 U were administered twice daily over a period of three days and heparin activity was controlled before injection and 2,4,8 hours afterwards by means of the APTT, the anti-Xa clotting test and a chromogenic substrate assay. In addition, the in vivo effect of fractionated heparin on platelet function was examined. The results show that the LMW fraction induced markedly higher anti-Xa activity than the other preparations. At the same time, APTT results did not significantly differ. Unfractionated heparin and the HMW fraction enhanced ADP-induced platelet aggregation and collagen-mediated MDA-production, while the LMW fraction hardly affected these assays, but potently inhibited thrombin-induced MDA production. All heparin preparations stimulated the release of PF IV, whereas the serotonin content of platelets determined at the same time increased.It is concluded that s.c. injections of LMW heparin induce relatively high levels of anti-Xa activity without leading to sensitive platelet activation or to major effects on overall clotting tests.

scholarly journals Adsorption of F VIII on Aluminium Hydroxide

1977 ◽  
Author(s):  
M. J. Seghatchian ◽  
T. Barrowcliffe ◽  
M. Miller-Andersson
Keyword(s):  
Molecular Weight ◽  
High Purity ◽  
Aluminium Hydroxide ◽  
Gel Filtration ◽  
Procoagulant Activity ◽  
Void Volume ◽  
Low Molecular Weight ◽  
Two Stage ◽  
Volume Fractions ◽  
High Purification

Adsorption of plasma by A1(OH)3 is a requirement for the two stage assay of F VIII. It is generally accepted that factors II, VII, IX and X are removed by the procedure, while factors V and VIII are unaffected. Following gel filtration of a F VIII concentrat on Sepharose 4 B F VIII:c was found in the low molecular weight area, as well as in the void volume as expected. This activity was found with both one and two stage techniques. After adsorption of the fractions with Al(OH)3 to eliminate the non F VIII procoagulant activity F VIII:c disappeared from the void volume fractions and was much reduced in the low molecular region. F VIII: R Ag was also removed from these fractions by A1(OH)3 adsorption. After adsorption of fractions in the presence of hemophilia plasma clotting activity remained in both regions suggesting the presence of true F VIII activity. Thus at concentration of 1 IU of F VIII:c per ml, a low purity preparation was unaffected by A1(OH)3 adsorption whereas both antigen and clotting activity of a high purity concentrate were conciderably reduced. Addition of 5 % albumin to the high purity preparation prevented this adsorption. It is concluded that under conditions of high purification F VIII:c can be adsorbed preferentially on A1(OH)3 and this appears to be due to removal of F VIII:R Ag.

Sign in / Sign up

Export Citation Format

Share Document