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Journal ArticleDOI

Protein binding of drugs in uremic and normal serum: The role of endogenous binding inhibitors

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TLDR
The protein binding of diazepam, indomethacin, salicylic acid, sulfadimetoxine and warfarin in serum of uremic patients has been studied by equilibrium dialysis and circular dichroism measurements and compared with that in normal serum.
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This article is published in Biochemical Pharmacology.The article was published on 1976-05-15. It has received 177 citations till now. The article focuses on the topics: Serum albumin & Human serum albumin.

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Citations
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Journal ArticleDOI

Disease-induced Changes in the Plasma Binding of Basic Drugs

TL;DR: Plasma concentration monitoring of drug therapy by use of total drug concentrations will be inaccurate in situations in which large variations in binding occur, and misinterpretations of both therapeutic monitoring and pharmacokinetic studies in disease slates with altered binding are likely.
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Increased plasma protein binding of propranolol and chlorpromazine mediated by disease-induced elevations of plasma alpha1 acid glycoprotein.

TL;DR: Increases in plasma protein binding in patients with inflammatory disease appear mediated by increases in alpha1 acid glycoprotein concentration, which may influence drug kinetics.
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Clinical pharmacokinetics of alfentanil, fentanyl and sufentanil. An update.

TL;DR: Alfentanil has the most rapid analgesic onset and time to peak effect as well as the shortest distribution and elimination half-lives, while the volume of distribution and total body clearance of this agent are smaller when compared with those of fentanyl and sufentanin.
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Clinical pharmacokinetics of phenytoin.

TL;DR: The metabolism of Phenytoin to the major metabolite, 5-(p-hydroxyphenyl)-5-(phenylhydantoin, is saturable, giving rise to a non linear dose-serum concentration relationship, so the dose range compatible with a therapeutic serum concentration is narrow within subjects, and monitoring serum concentrations is of particular value in dosage tailoring.
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Protein binding as a primary determinant of the clinical pharmacokinetic properties of non-steroidal anti-inflammatory drugs.

TL;DR: The clinical pharmacokinetic properties of future NSAIDs which emerge from the same chemical classes as currently available NSAIDs can be expected to be profoundly influenced by the extent and affinity of binding of the drugs to proteins.
References
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Journal ArticleDOI

The Attractions of Proteins for Small Molecules and Ions

TL;DR: The number and variety of known compounrjs between proteins and small molecules are increasing rapidly and make a fascinating story as discussed by the authors, and there are many compounds of serum albumin, which was used during the war by many chemists, most of whom found at least one 6ew compound.
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Immunochemical quantitation of antigens by single radial immunodiffusion

TL;DR: By standardizing the technical conditions of the experiment it is possible to use this principle for the immunochemical determination of antigens, and the lower limit of the method was found to correspond to 0·0025 μg of antigen, and to an antigen concentrations of 1·25 μg per ml.
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Removal of Fatty Acids from Serum Albumin by Charcoal Treatment

TL;DR: Fluorescence spectra of human serum albumin samples indicated that impurities are sometimes present which can be removed by charcoal at neutral pH, and acid-charcoal treatment is a much more rapid method of removing lipid impurities than other methods previously described.
Journal ArticleDOI

Determination of serum creatinine by a direct colorimetric method.

TL;DR: A method has been elaborated permitting serum creatinine determination without prior deproteinisation, and values are obtained that correlate well to those obtained with a method involving isolation of Creatinine with a chromatographic procedure.
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Protein binding of diphenylhydantoin and desmethylimipramine in plasma from patients with poor renal function.

TL;DR: The binding of DPH by plasma proteins from azotemic patients appears to be decreased, probably owing to a change in the binding proteins.
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