Octafluorotoluene as a derivatizing agent for steroids in human plasma

1988 ◽  
Vol 16 (1-12) ◽  
pp. 211-213 ◽  
Author(s):  
Michael H. Baker ◽  
Ian Howe ◽  
Michael Jarman ◽  
Raymond McCague
Keyword(s):  
Human Plasma ◽  
Derivatizing Agent

Analysis of 26 amino acids in human plasma by HPLC using AQC as derivatizing agent and its application in metabolic laboratory

Amino Acids ◽  
2014 ◽  
Vol 46 (5) ◽  
pp. 1253-1263 ◽  
Author(s):  
Gaurav Sharma ◽  
Savita Verma Attri ◽  
Bijaylaxmi Behra ◽  
Swapnil Bhisikar ◽  
Praveen Kumar ◽  
...  
Keyword(s):  
Amino Acids ◽  
Human Plasma ◽  
Derivatizing Agent

BIOANALYTICAL METHOD DEVELOPMENT AND VALIDATION OF MEMANTINE HYDROCHLORIDE BY SPECTROFLUORIMETRIC METHOD USING OPA Β-MERCAPTOETHANOL AS DERIVATIZING AGENT

INDIAN DRUGS ◽  
2014 ◽  
Vol 51 (09) ◽  
pp. 12-16
Author(s):  
C. B Patel ◽  
◽  
C. S. Kothari ◽  
N. R Patel ◽  
O Sherikar
Keyword(s):  
Human Plasma ◽  
Method Development ◽  
High Recovery ◽  
Synchronous Mode ◽  
Liquid Liquid Extraction ◽  
Spectrofluorimetric Method ◽  
Derivatizing Agent ◽  
Method Development And Validation ◽  
Development And Validation

A new, simple, accurate, sensitive and specific bioanalytical spectrofluorimetric method was developed and validated for estimation of memantine hydrochloride (MEM) in human plasma. Estimation of MEM in human plasma was done by spiked human plasma studies. Extraction of MEM from human plasma was carried out using 5% trichloroacetic acid for protein precipitation followed by liquid-liquid extraction with 5% IPA in n-hexane. For spectrofluorimetric estimation delta value 65 applied in synchronous mode (medium sensitivity mode) and fluorescence intensity was measured at 420 nm. Developed method was found linear to be in the concentration range of 50-300 ng/mL with correlation coefficient (R2) 0.9951. Percentage recovery was found to be 77.85-83.68% for MEM. High recovery shows that the method is free from the interference from plasma constituents. Hence, proposed method can be used for estimation of MEM in routine quality control laboratories for quantitative determination of MEM in bulk as well as in human plasma. Further it can also be used to determine plasma MEM concentration in drug monitoring or in pharmacokinetic investigations.

Performances of an Artificial Reagent for the One-stage Factor IX Assay

1975 ◽  
Vol 33 (03) ◽  
pp. 547-552 ◽  
Author(s):  
L Meunier ◽  
J. P Allain ◽  
D Frommel
Keyword(s):  
Human Plasma ◽  
Factor Ix ◽  
Severe Haemophilia ◽  
Normal Human Plasma ◽  
Haemophilia B ◽  
One Stage ◽  
Normal Human ◽  
The One

SummaryA mixture of adsorbed normal human plasma and chicken plasma was prepared as reagent for factor IX measurement using a one-stage method. The substrate was found to be specific for factor IX. Its performances tested on samples displaying factor IX activity ranging from <l%–2,500% compared favorably with those obtained when using the plasma of severe haemophilia B patients as substrate.

Plasma Components which Interfere with Ristocetin-induced Platelet Aggregation

1975 ◽  
Vol 33 (03) ◽  
pp. 540-546 ◽  
Author(s):  
Robert F Baugh ◽  
James E Brown ◽  
Cecil Hougie
Keyword(s):  
Platelet Aggregation ◽  
Human Plasma ◽  
Plasma Proteins ◽  
Binding Protein ◽  
Plasma Heating ◽  
Protein S ◽  
Fold Increase ◽  
Normal Human Plasma ◽  
Preliminary Examination ◽  
Normal Human

SummaryNormal human plasma contains a component or components which interfere with ristocetin-induced platelet aggregation. Preliminary examination suggests a protein (or proteins) which binds ristocetin and competes more effectively for ristocetin than do the proteins involved in ristocetin-induced platelet aggregation. The presence of this protein in normal human plasma also prevents ristocetin-induced precipitation of plasma proteins at levels of ristocetin necessary to produce platelet aggregation (0.5–2.0 mg/ml). Serum contains an apparent two-fold increase of this component when compared with plasma. Heating serum at 56° for one hour results in an additional 2 to 4 fold increase. The presence of a ristocetin-binding protein in normal human plasma requires that this protein be saturated with ristocetin before ristocetin-induced platelet aggregation will occur. Variations in the ristocetin-binding protein(s) will cause apparent discrepancies in ristocetin-induced platelet aggregation in normal human plasmas.

Studies on the Fibrinolytic System in Human Plasma: Quantitative Determination of Plasminogen Activators and Proactivators

1979 ◽  
Vol 41 (02) ◽  
pp. 365-383 ◽  
Author(s):  
C Kluft
Keyword(s):  
Pilot Study ◽  
Plasma Level ◽  
Human Plasma ◽  
Plasminogen Activators ◽  
Venous Occlusion ◽  
Quantitative Information ◽  
Optimal Recovery ◽  
Dextran Sulphate ◽  
Baseline Levels

SummaryEffects due to plasma plasminogen activators and proactivators are usually studied in assay systems where inhibitors influence the activity and where the degree of activation of proactivators is unknown. Quantitative information on activator and proactivator levels in plasma is therefore not availableStudies on the precipitating and activating properties of dextran sulphate in euglobulin fractionation presented in this paper resulted in the preparation of a fraction in which there was optimal recovery and optimal activation of a number of plasminogen activators and proactivators from human plasma. The quantitative assay of these activators on plasminogen-rich fibrin plates required the addition of flufenamate to eliminate inhibitors. The response on the fibrin plates (lysed zones) could be coverted to arbitrary blood activator units (BAU). Consequently, a new activator assay which enables one to quantitatively determine the plasma level of plasminogen activators and proactivators together is introduced.Two different contributions could be distinguished: an activity originating from extrinsic activator and one originating from intrinsic proactivators. The former could be assayed separately by means of its resistance to inhibition by Cl-inactivator. Considering the relative concentrations of extrinsic and intrinsic activators, an impression of the pattern of activator content in plasma was gained. In morning plasma with baseline levels of fibrinolysis, the amount of extrinsic activator was negligible as compared to the level of potentially active intrinsic activators. Consequently, the new assay nearly exclusively determines the level of intrinsic activators in morning plasma. A pilot study gave a fairly stable level of 100 ± 15 BAU/ml (n = 50). When fibrinolysis was stimulated by venous occlusion (15 min), the amount of extrinsic activator was greatly increased, reaching a total activator level of 249 ± 27 BAU/ml (n = 7).

Potentially Thrombogenic Materials in Factor IX Concentrates

1975 ◽  
Vol 33 (03) ◽  
pp. 617-631 ◽  
Author(s):  
H. S Kingdon ◽  
R. L Lundblad ◽  
J. J Veltkamp ◽  
D. L Aronson
Keyword(s):  
Human Plasma ◽  
Antithrombin Iii ◽  
Factor Ix ◽  
In Vitro Assays ◽  
Substantial Agreement ◽  
Coefficient Of Correlation

SummaryFactor IX concentrates manufactured from human plasma and intended for therapeutic infusion in man have been suspected for some time of being potentially thrombogenic. In the current studies, assays were carried out in vitro and in vivo for potentially thrombogenic materials. It was possible to rank the various materials tested according to the amount of thrombogenic material detected. For concentrates not containing heparin, there was substantial agreement between the in vivo and in vitro assays, with a coefficient of correlation of 0.77. There was no correlation between the assays for thrombogenicity and the antithrombin III content. We conclude that many presently available concentrates of Factor IX contain substantial amounts of potentially thrombogenic enzymes, and that this fact must be considered in arriving at the decision whether or not to use them therapeutically.

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