In situ determination of high hydrogen ion concentrations in aqueous solutions using a Nafion membrane containing Rhodamine 6G

The Analyst ◽  
1993 ◽  
Vol 118 (7) ◽  
pp. 929 ◽  
Author(s):  
Hari Mohan ◽  
R. M. lyer
Keyword(s):  
Aqueous Solutions ◽  
Rhodamine 6G ◽  
Hydrogen Ion ◽  
Nafion Membrane ◽  
High Hydrogen ◽  
Ion Concentrations

scholarly journals THE INACTIVATION OF COMPLEMENT AND ITS COMPONENTS BY PLASMIN

1953 ◽  
Vol 97 (4) ◽  
pp. 573-589 ◽  
Author(s):  
Louis Pillemer ◽  
Oscar D. Ratnoff ◽  
Livia Blum ◽  
I. H. Lepow
Keyword(s):  
Human Serum ◽  
Proteolytic Enzyme ◽  
Complement Fixation ◽  
Hydrogen Ion ◽  
Complement Components ◽  
High Hydrogen ◽  
Ion Concentrations ◽  
Plasmin Inhibitors ◽  
Antigen Antibody

Human complement is inactivated by plasmin, the proteolytic enzyme of plasma or serum active at or near neutrality. The addition of streptokinase to human serum, which converts plasminogen to plasmin, also causes the inactivation of complement components C'2 and C'4 and varying amounts of C'1. C'3 is the most resistant to inactivation by plasmin. Chloroform-activated human plasmin and bovine plasmin also destroy these components of complement, but are less effective than the streptokinase-activated enzyme. The inactivation of complement by the addition of streptokinase to human serum is inhibited by high hydrogen ion concentrations, low temperature, and elevated ionic strength. The inactivation of the components of complement in various fractions of serum is influenced by the available plasminogen and the content of plasmin inhibitors in these fractions. Certain similarities are pointed out between the components of complement and the factors in the plasmin system and between the inactivation of the components of complement by antigen-antibody reactions, by specific agents, and by plasmin. The possible significance of these relationships in immune hemolysis and complement fixation, and the possible role of the plasmin system in the instability of complement and the development of anticomplementary properties in serum are discussed.

scholarly journals Study of Errors in Determination of Hydrogen Ion Concentrations in Rainwater Samples Using Glass Electrode Method.

1998 ◽  
Vol 14 (4) ◽  
pp. 749-756 ◽  
Author(s):  
Toru OZEKI ◽  
Yasuo TSUBOSAKA ◽  
Shizu NAKAYAMA ◽  
Nobuaki OGAWA ◽  
Takashi KIMOTO
Keyword(s):  
Glass Electrode ◽  
Hydrogen Ion ◽  
Ion Concentrations ◽  
Electrode Method

THE SOLVENT EXTRACTION OF PROTACTINIUM

1956 ◽  
Vol 34 (3) ◽  
pp. 284-292 ◽  
Author(s):  
A. Goble ◽  
J. Golden ◽  
A. G. Maddock
Keyword(s):  
Nitric Acid ◽  
Solvent Extraction ◽  
Hydrochloric Acid ◽  
Aqueous Solutions ◽  
Aqueous Phase ◽  
Hydrogen Ion ◽  
Nitrate Complex ◽  
Constant Concentration ◽  
Extraction Coefficient ◽  
Ion Concentrations

The variation of the experimental extraction coefficient for protactinium upon dilution of the solvent ketone with benzene has been determined for aqueous solutions at constant concentration of hydrochloric acid. The bromo complex has been shown to be far less readily extracted. The effects on the extraction of the nitrate complex by amyl acetate, of the nitric acid, of the nitrate and hydrogen ion concentrations in the aqueous phase, as well as of the dilution of the solvent with benzene, have been explored. The existence of a slow reaction in the extraction has been demonstrated. It is concluded that chloride solutions are the more reliable for the isolation of protactinium from concentrates.

Some Distinctive Characteristics of the Alkaline Phosphatase of Serratia marcescens

1975 ◽  
Vol 53 (7) ◽  
pp. 819-822 ◽  
Author(s):  
A. R. Bhatti
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Serratia Marcescens ◽  
Heat Stability ◽  
Hydrogen Ion ◽  
High Hydrogen ◽  
E Coli ◽  
Ion Concentrations ◽  
Enzyme Species

A mutant strain of Serratia marcescens produces a constitutive enzyme (phosphatase F) which differs from the alkaline phosphatase of Escherichia coli in the following characteristics: one enzyme species with higher mobility on electrophoresis, less heat stability, no rapid reactivation following exposure to high hydrogen ion concentrations, no hybridization with E. coli enzyme in vitro, little activation at increased ionic strength, greater sensitivity to EDTA inhibition, and no cross reaction of rabbit anti-serum with the E. coli enzyme.

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