Variations in protein binding of drugs in plasma and serum.

1989 ◽  
Vol 35 (8) ◽  
pp. 1722-1725 ◽  
Author(s):  
T Ohshima ◽  
T Hasegawa ◽  
I Johno ◽  
S Kitazawa
Keyword(s):  
Protein Binding ◽  
Free Fraction ◽  
Physiological Data ◽  
Protein Patterns ◽  
Two Dimensional Electrophoresis ◽  
Phenytoin Sodium ◽  
Protein Binding Of Drugs ◽  
Dimensional Electrophoresis ◽  
Better Than

Abstract The free fractions of five drugs were determined in plasma treated with EDTA and in serum. The free fractions of phenytoin, sodium valproate, and phenobarbital in serum were significantly higher than in plasma (P less than 0.05). In contrast, the free fractions of carbamazepine and theophylline were significantly lower in serum than in plasma. Although we observed minor differences in the protein patterns obtained with two-dimensional electrophoresis, these did not have an important influence on protein binding. No significant differences were observed between plasma and serum in the physiological data, except for pH. Binding of these drugs by protein was shown to be pH-dependent. We conclude that serum may be better than plasma for determination of the free fraction, because the free fraction in plasma is affected by anticoagulants such as EDTA salts and heparin.

scholarly journals AUTOMATIC SELECTION OF TWO-DIMENSIONAL ELECTROPHORESIS GEL WITH LEAST GEOMETRIC DISTORTIONS

2010 ◽  
Vol 2 (1) ◽  
pp. 9-13
Author(s):  
Dalius Matuzevičius
Keyword(s):  
Quality Criterion ◽  
Horizontal Line ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Two Dimensional Electrophoresis ◽  
Geometric Distortions ◽  
Biochemical Experiment ◽  
Dimensional Electrophoresis ◽  
Selection Of

The paper presents an algorithm for automated selection of the highest quality two-dimensional gel electrophoresis image. The quality criterion is the amount of vertical geometric distortions of the gel. The aim is to select the least distorted gel from the group received during the same biochemical experiment. Vertical geometric distortions displace proteins of the same molecular mass from the horizontal line and have a greater impact on the determination of protein characteristics than horizontal distortions. After presenting algorithm for evaluation of distortions and selection of base gel results are compared to expert's made selections. If necessary, algorithm may be adapted for horizontal distortion evaluation.

scholarly journals Identification of two major proteins of bovine pancreatic stones as immunoreactive forms of trypsinogens

1982 ◽  
Vol 205 (3) ◽  
pp. 543-549 ◽  
Author(s):  
A De Caro ◽  
L Multigner ◽  
H Vérine
Keyword(s):  
Molecular Weight ◽  
Isoelectric Focusing ◽  
Sodium Citrate ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Charge Heterogeneity ◽  
Two Dimensional Electrophoresis ◽  
Pancreatic Stones ◽  
Dimensional Electrophoresis

Two major proteins have been identified in sodium citrate extracts of bovine pancreatic stones from 15 glands with lithiasis. They were found to have a molecular weight of about 24 000 and were further characterized by a variety of methods, including polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate, isoelectric focusing, two-dimensional electrophoresis, immunodiffusion, immunoelectrophoresis and determination of N-terminal residues. These two immunologically and electrophoretically different proteins were definitely shown to be immunoreactive forms of anionic and cationic trypsinogens, which are normal components of pancreatic juice. However, in contrast with both secretory trypsinogens, the stone proteins displayed an important charge heterogeneity under isoelectric-focusing conditions. A possible role for both secretory trypsinogens in pancreatic lithogenesis is suggested by the reproducibility of the data. Finally, two minor proteins with a lower molecular weight (about 11 000-13 000) have also been found to be present in all extracts, but have not yet been identified.

Plasma apolipoprotein pattern in fish-eye disease examined by high-resolution two-dimensional electrophoresis.

1985 ◽  
Vol 31 (12) ◽  
pp. 2032-2035 ◽  
Author(s):  
T Marshall ◽  
K M Williams ◽  
L Holmquist ◽  
L A Carlson ◽  
O Vesterberg
Keyword(s):  
High Resolution ◽  
Plasma Proteins ◽  
Eye Disease ◽  
Two Dimensional ◽  
Protein Patterns ◽  
Two Dimensional Electrophoresis ◽  
Significant Difference ◽  
Fish Eye ◽  
Dimensional Electrophoresis ◽  
Plasma Apolipoprotein

Abstract We compared the plasma protein patterns of the two living patients suffering from fish-eye disease with those of appropriate controls, using high-resolution two-dimensional electrophoresis. Quantitative abnormalities were detected in plasma polypeptides corresponding to the isoforms of apolipoproteins A-I and A-II. The disease was characterized by normal concentrations of proapo A-I but dramatically subnormal concentrations of the other apo A-I isoforms and apo A-II. No significant difference was detected in the concentrations of other plasma proteins. These findings are discussed in relation to other apolipoprotein disorders.

scholarly journals The Effect of Plasma Protein Binding on the Therapeutic Monitoring of Antiseizure Medications

Pharmaceutics ◽  
2021 ◽  
Vol 13 (8) ◽  
pp. 1208
Author(s):  
Bruno Charlier ◽  
Albino Coglianese ◽  
Federica De Rosa ◽  
Ugo de Grazia ◽  
Francesca Felicia Operto ◽  
...  
Keyword(s):  
Protein Binding ◽  
Biological Fluids ◽  
Free Fraction ◽  
Inhibitory Response ◽  
Therapeutic Monitoring ◽  
Therapeutic Drug ◽  
Toxicological Effects ◽  
Action Mechanisms ◽  
Methodological Aspects

Epilepsy is a widely diffused neurological disorder including a heterogeneous range of syndromes with different aetiology, severity and prognosis. Pharmacological treatments are based on the use, either in mono- or in polytherapy, of antiseizure medications (ASMs), which act at different synaptic levels, generally modifying the excitatory and/or inhibitory response through different action mechanisms. To reduce the risk of adverse effects and drug interactions, ASMs levels should be closely evaluated in biological fluids performing an appropriate Therapeutic Drug Monitoring (TDM). However, many decisions in TDM are based on the determination of the total drug concentration although measurement of the free fraction, which is not bound to plasma proteins, is becoming of ever-increasing importance since it correlates better with pharmacological and toxicological effects. Aim of this work has been to review methodological aspects concerning the evaluation of the free plasmatic fraction of some ASMs, focusing on the effect and the clinical significance that drug-protein binding has in the case of widely used drugs such as valproic acid, phenytoin, perampanel and carbamazepine. Although several validated methodologies are currently available which are effective in separating and quantifying the different forms of a drug, prospective validation studies are undoubtedly needed to better correlate, in real-world clinical contexts, pharmacokinetic monitoring to clinical outcomes.

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