scholarly journals Microbiological pollution and some physicochemical properties of sıkaraağaçlar creek in sinop (Black Sea-Turkey)

2020 ◽  
Vol 41 (3) ◽  
pp. 580-593
Author(s):  
Ayşe GÜNDOĞDU ◽  
Uğur ÇARLI
Keyword(s):  
Physicochemical Properties ◽  
Black Sea ◽  
Microbiological Pollution

Preparation and characterisation of vanadium pentoxide supported rhodium catalyst

1988 ◽  
Vol 46 ◽  
pp. 946-947
Author(s):  
A. Legrouri
Keyword(s):  
Aqueous Solution ◽  
Thermal Decomposition ◽  
Physicochemical Properties ◽  
Surface Area ◽  
Vanadium Pentoxide ◽  
High Purity ◽  
Gas Adsorption ◽  
Rhodium Catalyst ◽  
Optical Methods ◽  
Reducible Oxides

The industrial importance of metal catalysts supported on reducible oxides has stimulated considerable interest during the last few years. This presentation reports on the study of the physicochemical properties of metallic rhodium supported on vanadium pentoxide (Rh/V2O5). Electron optical methods, in conjunction with other techniques, were used to characterise the catalyst before its use in the hydrogenolysis of butane; a reaction for which Rh metal is known to be among the most active catalysts.V2O5 powder was prepared by thermal decomposition of high purity ammonium metavanadate in air at 400 °C for 2 hours. Previous studies of the microstructure of this compound, by HREM, SEM and gas adsorption, showed it to be non— porous with a very low surface area of 6m2/g3. The metal loading of the catalyst used was lwt%Rh on V2Q5. It was prepared by wet impregnating the support with an aqueous solution of RhCI3.3H2O.

MÖSSBAUER AND CHEMICAL ANALYSES OF SOME SEDIMENTS FROM THE ROMANIAN SHORE OF THE BLACK SEA

1979 ◽  
Vol 40 (C2) ◽  
pp. C2-445-C2-448
Author(s):  
D. Barb ◽  
L. Diamandescu ◽  
M. Morariu ◽  
I. I. Georgescu
Keyword(s):  
Black Sea ◽  
The Black Sea ◽  
Chemical Analyses

Studies on the Degradation of Human Fibrinogen by Plasmin and Trypsin

1966 ◽  
Vol 16 (03/04) ◽  
pp. 526-540 ◽  
Author(s):  
E. A Beck ◽  
D. P Jackson
Keyword(s):  
Physicochemical Properties ◽  
Electrophoretic Mobility ◽  
Rapid Loss ◽  
Clotting System ◽  
Human Fibrinogen ◽  
Peptide Bonds ◽  
Physico Chemical ◽  
Starch Gel ◽  
Ph Stat ◽  
Rapid Appearance

SummaryThe effects of trypsin and plasmin on the functional and physicochemical properties of purified human fibrinogen were observed at various stages of proteolysis. Concentrations of plasmin and trypsin that produced fibrinogenolysis at comparable rates as measured in a pH stat produced, at similar rates, loss of precipitability of fibrinogen by heat and ammonium sulphate and alterations in electrophoretic mobility on starch gel. Trypsin produced a more rapid loss of clottability of fibrinogen and a more rapid appearance of inhibitors of the thrombin-fibrinogen clotting system than did plasmin. Consistent differences were noted between the effects of trypsin and plasmin on the immunoelectrophoretic properties of fibrinogen during the early stages of proteolysis.These results are consistent with the hypothesis that trypsin initially reacts with the same peptide bonds of fibrinogen that are split by thrombin, but these same bonds do not appear to be split initially by plasmin. Measurement of the various functional and physico-chemical changes produced by the action of trypsin and plasmin on fibrinogen can be used to recognize various stages of proteolysis.

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