A Resolution Equation for Electrokinetic Chromatography Based on Electrophoretic Mobilities

1995 ◽  
Vol 67 (17) ◽  
pp. 2966-2973 ◽  
Author(s):  
Jeffrey R. Mazzeo ◽  
Michael E. Swartz ◽  
Edward R. Grover
Keyword(s):  
Electrokinetic Chromatography ◽  
Résolution Équation ◽  
Electrophoretic Mobilities

Identification of Fibrinogen Derivatives in Plasma Samples

1972 ◽  
Vol 27 (03) ◽  
pp. 610-618 ◽  
Author(s):  
H Graeff ◽  
R von Hugo
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Gel Chromatography ◽  
Agarose Gel ◽  
Plasma Samples ◽  
Methodological Study ◽  
Parent Molecule ◽  
Electrophoretic Mobilities ◽  
Fibrin Monomer

SummaryThe observation of fibrinogen derivatives with a molecular weight higher than the parent molecule in human cases of DIC initiated the present methodological study. These derivatives were identified by the following methods : 2.5 M β-alanine precipitation of the plasma samples, PAA gel electrophoresis, intra gel immunoprecipitation and agarose gel chromatography. In the plasma of a patient with severe eclampsia and laboratory signs of DIC two derivatives with a molecular weight higher than that of fibrinogen were identified according to their relative electrophoretic mobilities: 0.18 and 0.28 × 10−5 cm2/V × sec (fibrinogen: 0.43 × 10−5 cm2/V × sec). Electrophoretic studies in the presence of 5 M urea indicated that the 0.28 derivative is a complex probably formed by fibrinogen and a fibrin monomer.

Bovine Platelet Proteins III. Some Properties of Platelet Fibrinogen

1969 ◽  
Vol 21 (03) ◽  
pp. 428-440 ◽  
Author(s):  
N. O Solum ◽  
S Łopaciuk
Keyword(s):  
Intrinsic Viscosity ◽  
Rabbit Antiserum ◽  
Disc Electrophoresis ◽  
Carbohydrate Content ◽  
Plasma Fibrinogen ◽  
Total Amino Acid ◽  
Electrophoretic Mobilities ◽  
Bovine Plasma ◽  
Starch Gel ◽  
The Difference

Summary1. Some properties of purified bovine platelet fibrinogen have been described and the data compared to those obtained by parallel analysis of purified bovine plasma fibrinogen.2. A close similarity was found between platelet and plasma fibrinogen as to sedimentation coefficients, electrophoretic mobilities in starch gel and polyacrylamide disc electrophoresis, light absorption spectra in the range 240 mμ to 330 mμ, ability to form immunoprecipitate with a rabbit antiserum against bovine plasma fibrinogen, total amino acid composition and in N-terminal amino acids.Differences between the fibrinogens were found as to intrinsic viscosity, carbohydrate content and behaviour upon clotting by thrombin. Intrinsic viscosity in 0.3 M NaCl at 25° was 0.48 dl/g for platelet fibrinogen as compared to 0.26 dl/g for plasma fibrinogen. The carbohydrate content of platelet fibrinogen was 0.56 ± 0.10% 1.56±0.10% and 1.37±0.09% for sialic acid (calculated as N-glycolyl neuraminic acid), hexose (galactose/mannose 1:2) and hexosamine (glucosamine), respectively. These values were 6, 54 and 26% higher than those found for plasma fibrinogen. The difference in clotting behaviour indicated a slower polymerization rate of the fibrin monomers formed from platelet fibrinogen than of those formed from plasma fibrinogen.

Determination of Imipenem and Cilastatin in Medicinal Products by Micellar Electrokinetic Chromatography

2017 ◽  
Vol 13 (2) ◽  
pp. 158-166 ◽  
Author(s):  
Tyski Stefan ◽  
Gruba Ewa ◽  
Bukowska Bozena ◽  
Michalska Katarzyna ◽  
Karpiuk Izabela
Keyword(s):  
Micellar Electrokinetic Chromatography ◽  
Electrokinetic Chromatography ◽  
Medicinal Products

Quantitative Analysis of Duloxetine and 1-Naphthol by Capillary Micellar Electrokinetic Chromatography

2011 ◽  
Vol 7 (3) ◽  
pp. 184-193 ◽  
Author(s):  
Nathalie R. Wingert ◽  
Aline B. Barth ◽  
Patricia Gomes ◽  
Elfrides E. S. Shapoval ◽  
Martin Steppe
Keyword(s):  
Quantitative Analysis ◽  
Micellar Electrokinetic Chromatography ◽  
Electrokinetic Chromatography

scholarly journals A shift in the optimum pH of phospholipase D produced by activating long-chain anions

1969 ◽  
Vol 112 (5) ◽  
pp. 795-799 ◽  
Author(s):  
R. H. Quarles ◽  
R. M. C. Dawson
Keyword(s):  
Phosphatidic Acid ◽  
Phospholipase D ◽  
Activity Profile ◽  
Ph Optimum ◽  
Surface Ph ◽  
Electrophoretic Mobilities ◽  
Low Concentrations ◽  
Optimum Ph ◽  
Long Chain

1. The activity of phospholipase D (phosphatidylcholine phosphatidohydrolase, EC 3.1.4.4) towards ultrasonically treated phosphatidylcholine or large phosphatidylcholine particles activated with ether was maximal near pH5, and there was little activity above pH6. 2. When the enzyme was activated by the addition of phosphatidic acid to large phosphatidylcholine particles the pH optimum was shifted to pH6·5 irrespective of the amount of activator added. 3. When the enzyme was activated with low concentrations of dodecyl sulphate the pH optimum was 5·5 with little activity above pH6. With higher concentrations of dodecyl sulphate the pH–activity profile was shifted upwards towards a pH optimum of 6·5–6·6, the magnitude of the shift depending on the extent of the hydrolysis. 4. The shifts in the pH–activity profiles cannot be correlated with changes in the ‘surface pH’ of the substrate particles calculated from the measurement of their ζ-potentials (electrophoretic mobilities).

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