The enantioselective metabolic mechanism of quizalofop-ethyl and quizalofop-acid enantiomers in animal: protein binding, intestinal absorption, and in vitro metabolism in plasma and the microsome

RSC Advances ◽  
2016 ◽  
Vol 6 (101) ◽  
pp. 99003-99009
Author(s):  
Yiran Liang ◽  
Peng Wang ◽  
Donghui Liu ◽  
Jing Zhan ◽  
Mai Luo ◽  
...  
Keyword(s):  
Serum Albumin ◽  
Protein Binding ◽  
Intestinal Absorption ◽  
Liver Microsome ◽  
Animal Protein ◽  
In Vitro Metabolism ◽  
Everted Gut Sac ◽  
Metabolic Mechanism ◽  
Quizalofop Ethyl

The effects of protein binding (pepsin, trypsin and serum albumin), intestinal absorption (everted gut sac), and degradation (plasma, liver microsome and cytosol) on the enantioselectivity of quizalofop-ethyl in animals were studiedin vitro.

Evaluation of oral pharmacokinetics, in vitro metabolism, blood partitioning and plasma protein binding of novel antidiabetic agent, S009-0629 in rats

2018 ◽  
Vol 79 (4) ◽  
pp. 173-183 ◽  
Author(s):  
Guru Raghavendra Valicherla ◽  
Kishan Shamjibhai Italiya ◽  
Chandra Prakash Gupta ◽  
Shachi Mishra ◽  
Mohammed Riyazuddin ◽  
...  
Keyword(s):  
Protein Binding ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
In Vitro Metabolism ◽  
Antidiabetic Agent ◽  
Oral Pharmacokinetics

Estrogen-induced Changes in Protein Binding of Bupivacaine during in Vitro Fertilization 

1997 ◽  
Vol 87 (4) ◽  
pp. 879-883 ◽  
Author(s):  
Lawrence C. Tsen ◽  
G. Richard Arthur ◽  
Sanjay Datta ◽  
Mark D. Hornstein ◽  
Angela M. Bader
Keyword(s):  
In Vitro Fertilization ◽  
Serum Albumin ◽  
Protein Binding ◽  
Serum Proteins ◽  
Free Fraction ◽  
Vitro Fertilization ◽  
Acid Glycoprotein ◽  
Hormonal Manipulation ◽  
Bupivacaine Toxicity

Background Patients having in vitro fertilization (IVF) procedures that use gonadotropin-releasing hormone agonist down-regulation undergo hormonal manipulation of estrogen concentrations to induce oocyte maturation. After achieving minimal estrogen concentrations (baseline), stimulation increases estrogen concentrations to supraphysiologic levels, leading to egg retrieval. The isolated effect of estrogen on protein binding has not previously been reported. This study was conducted to measure the effect of estrogen concentrations on protein binding of two concentrations of bupivacaine, 1 microg/ml and 5 microg/ml, corresponding, respectively, to systemic concentrations expected after administration of epidural anesthesia and associated with bupivacaine toxicity. Serum proteins were measured to address the mechanism. Methods Twenty-nine healthy women undergoing IVF procedures were enrolled and venous samples were drawn at times of minimal and maximal estrogen concentrations. The percentage of free bupivacaine was determined at fixed concentrations of 1 and 5 microg/ml. Serum albumin and alpha1-acid glycoprotein concentrations were measured at baseline and at retrieval in a group of 24 women. Results The percentage of free bupivacaine increased between times of minimal and maximal serum estrogen concentrations, corresponding to decreased protein binding. Concentrations of serum albumin and alpha1-acid glycoprotein decreased between baseline and retrieval times. Conclusions Patients undergoing IVF procedures demonstrate a decrease in protein binding of bupivacaine from baseline concentrations. These changes may be explained by a decrease in albumin and alpha1-acid glycoprotein. During anesthesia for egg retrieval, clinicians should consider the implications of increased free fraction of drug, especially for highly protein-bound agents.

scholarly journals Pharmacokinetic properties, in vitro metabolism and plasma protein binding of govaniadine an alkaloid isolated from Corydalis govaniana Wall

2016 ◽  
Vol 131 ◽  
pp. 464-472 ◽  
Author(s):  
Lucas M.M. Marques ◽  
Daniel R. Callejon ◽  
Larissa G. Pinto ◽  
Michel L. de Campos ◽  
Anderson R.M. de Oliveira ◽  
...  
Keyword(s):  
Protein Binding ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
In Vitro Metabolism ◽  
Pharmacokinetic Properties

scholarly journals Characteristics of Dolutegravir and Bictegravir Plasma Protein Binding: a First Approach for the Study of Pharmacologic Sanctuaries

2020 ◽  
Vol 64 (11) ◽  
Author(s):  
Thibaut Gelé ◽  
Hélène Gouget ◽  
Valérie Furlan ◽  
Pierre-Hadrien Becker ◽  
Anne-Marie Taburet ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Protein Binding ◽  
Plasma Binding ◽  
Acid Glycoprotein ◽  
Binding Rate ◽  
Preferential Binding ◽  
High Protein Binding ◽  
Nonlinear Binding

ABSTRACT This study aimed to characterize in vitro dolutegravir (DTG) and bictegravir (BIC) binding. They had a preferential binding to human serum albumin (HSA) with two classes of albumin sites. Human alpha-1-acid glycoprotein (HAAG) binding of DTG and BIC showed an atypical nonlinear binding. The low-affinity site on HSA, the main plasma binding protein, suggests that the high protein binding rate should not impair passive diffusion.

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