Use of a Biophysical-Kinetic Model to Understand the Roles of Protein Binding and Membrane Partitioning on Passive Diffusion of Highly Lipophilic Molecules Across Cellular Barriers

1993 ◽  
Vol 1 (4) ◽  
pp. 269-286 ◽  
Author(s):  
Thomas Raub ◽  
Craig Barsuhn ◽  
Lawrence Williams ◽  
Douglas Decker ◽  
Geri Sawada ◽  
...  
Keyword(s):  
Kinetic Model ◽  
Protein Binding ◽  
Passive Diffusion ◽  
Membrane Partitioning

scholarly journals Preclinical Bioavailability, Tissue Distribution, and Protein Binding Studies of Erinacine A, a Bioactive Compound from Hericium erinaceus Mycelia Using Validated LC-MS/MS Method

Molecules ◽  
2021 ◽  
Vol 26 (15) ◽  
pp. 4510
Author(s):  
Pei-Ching Tsai ◽  
Yi-Kai Wu ◽  
Jun-Hao Hu ◽  
I-Chen Li ◽  
Ting-Wei Lin ◽  
...  
Keyword(s):  
Protein Binding ◽  
Tissue Distribution ◽  
Bioactive Compound ◽  
Passive Diffusion ◽  
Absolute Bioavailability ◽  
Sprague Dawley ◽  
Binding Studies ◽  
Hericium Erinaceus ◽  
Major Route ◽  
Erinacine A

Erinacine A, derived from the mycelia of Hericium erinaceus, has attracted much attention due to its neuroprotective properties. However, very few studies have been conducted on the bioavailability, tissue distribution, and protein binding of erinacine A. This study aimed to investigate the bioavailability, tissue distribution, and protein binding of erinacine A in Sprague-Dawley rats. After oral administration (po) and intravenous administration (iv) of 2.381 g/kg BW of the H. erinaceus mycelia extract (equivalent to 50 mg/kg BW of erinacine A) and 5 mg/kg BW of erinacine A, respectively, the absolute bioavailability of erinacine A was estimated as 24.39%. Erinacine A was detected in brain at 1 h after oral dosing and reached the peak at 8 h. Protein binding assay showed unbound erinacine A fractions in brain to blood ratio is close to unity, supporting passive diffusion as the dominating transport. Feces was the major route for the elimination of erinacine A. This study is the first to show that erinacine A can penetrate the blood-brain barrier of rats by the means of passive diffusion and thus support the development of H. erinaceus mycelia for the improvement of neurohealth.

Transient Prealbumin- Associated Hyperthyroxinemia in TSH-Producing Pituitary Adenoma

1990 ◽  
Vol 29 (01) ◽  
pp. 40-43 ◽  
Author(s):  
W. Langsteger ◽  
P. Költringer ◽  
P. Wakonig ◽  
B. Eber ◽  
M. Mokry ◽  
...  
Keyword(s):  
Computed Tomography ◽  
Case Report ◽  
Pituitary Adenoma ◽  
Thyroid Hormones ◽  
Protein Binding ◽  
Alpha Subunit ◽  
Normal Range ◽  
Thyroxine Binding Globulin ◽  
Free Thyroid Hormones ◽  
Transmission Computed Tomography

This case report describes a 38-year-old male who was hospitalized for further clarification of clinically mild hyperthyroidism. His increased total hormone levels, the elevated free thyroid hormones and the elevated basal TSH with blunted response to TRH strongly suggested a pituitary adenoma with inappropriate TSH incretion. Transmission computed tomography showed an intrasellar expansion, 16 mm in diameter. The neoplastic TSH production was confirmed by an elevated alpha-subunit and a raised molar alpha-sub/ATSH ratio. However, T4 distribution on prealbumin (PA, TTR), albumin (A) and thyroxine binding globulin (TBG) showed a clearly increased binding to PA (39%), indicating additional prealbumin-associated hyperthyroxinemia. The absolute values of PA, A and TBG were within the normal range. After removal of the TSH-producing adenoma, basal TSH, the free thyroid hormones and T4 binding to prealbumin returned to normal. Therefore, the prealbumin-associated hyperthyroxinemia had to be interpreted as a transitory phenomenon related to secondary hyperthyroidism (T4 shift from thyroxine binding globulin to prealbumin) rather than a genetically conditioned anomaly of protein binding.

Absorption, Metabolic Stability and Protein Binding Properties of Sutherlandioside B from Sutherlandia frutescens

Planta Medica ◽  
2008 ◽  
Vol 74 (03) ◽  
Author(s):  
VLM Madgula ◽  
B Avula ◽  
X Fu ◽  
XC Li ◽  
TJ Smillie ◽  
...  
Keyword(s):  
Protein Binding ◽  
Metabolic Stability ◽  
Binding Properties ◽  
Sutherlandia Frutescens

INCORPORATION OF IODIDE INTO ORGANIC COMPOUNDS IN THE GUINEA PIG THYROID

1963 ◽  
Vol 43 (1) ◽  
pp. 110-118 ◽  
Author(s):  
R. Ekholm ◽  
T. Zelander ◽  
P.-S. Agrell
Keyword(s):  
Guinea Pig ◽  
Protein Binding ◽  
Organic Compounds ◽  
Guinea Pigs ◽  
Microsomal Fraction ◽  
Thyroid Tissue ◽  
Particulate Fraction ◽  
Supernatant Fraction ◽  
Hydrolysis Of

ABSTRACT Guinea pigs, kept on a iodine-sufficient diet, were injected with Na131I and the thyroids excised from 45 seconds to 5 days later. The thyroid tissue was homogenized and separated into a combined nuclear-mitochondrial-microsomal fraction and a supernatant fraction by centrifugation at 140 000 g for one hour. Protein bound 131iodine (PB131I) and free 131iodide were determined in the fractions and the PB131I was analysed for monoiodotyrosine (MIT), diiodotyrosine (DIT) and thyroxine after hydrolysis of PB131I. As early as only 20 minutes after the Na131I-injection almost 100% of the particulate fraction 131I was protein bound. In the supernatant fraction the protein binding was somewhat less rapid and PB131I values above 90% of total supernatant 131I were not found until 3 hours after the injection. In all experiments the total amount of PB131I was higher in the supernatant than in the corresponding particulate fraction. The ratio between supernatant PB131I and pellet PB131I was lower in experiments up to 3 minutes and from 2 to 5 days than in experiments of 6 minutes to 20 hours. Hydrolysis of PB131I yielded, even in the shortest experiments, both MIT and DIT. The DIT/MIT ratio was lower in the experiments up to 2 hours than in those of 3 hours and over.

EVALUATION OF TISSUE STEROID BINDING IN VITRO

1971 ◽  
Vol 68 (1_Suppl) ◽  
pp. S223-S246 ◽  
Author(s):  
C. R. Wira ◽  
H. Rochefort ◽  
E. E. Baulieu
Keyword(s):  
Protein Binding ◽  
Binding Sites ◽  
Experimental System ◽  
Specific Protein ◽  
Coupling Mechanism ◽  
Target Tissue ◽  
Protein Binding Sites ◽  
Definition Of ◽  
Hormone Specificity

ABSTRACT The definition of a RECEPTOR* in terms of a receptive site, an executive site and a coupling mechanism, is followed by a general consideration of four binding criteria, which include hormone specificity, tissue specificity, high affinity and saturation, essential for distinguishing between specific and nonspecific binding. Experimental approaches are proposed for choosing an experimental system (either organized or soluble) and detecting the presence of protein binding sites. Techniques are then presented for evaluating the specific protein binding sites (receptors) in terms of the four criteria. This is followed by a brief consideration of how receptors may be located in cells and characterized when extracted. Finally various examples of oestrogen, androgen, progestagen, glucocorticoid and mineralocorticoid binding to their respective target tissues are presented, to illustrate how researchers have identified specific corticoid and mineralocorticoid binding in their respective target tissue receptors.

EVALUATION OF A SIMPLIFIED METHOD FOR DETERMINING SERUM THYROXINE BY COMPETITIVE PROTEIN BINDING ANALYSIS

1970 ◽  
Vol 64 (4) ◽  
pp. 630-636 ◽  
Author(s):  
Stephen C. Thorson ◽  
Ronald Tsujikawa ◽  
James L. Brown ◽  
Robert T. Morrison ◽  
Hamish W. McIntosh
Keyword(s):  
Protein Binding ◽  
Clinical Application ◽  
Thyroid Status ◽  
Serum Thyroxine ◽  
Binding Analysis ◽  
Simplified Method ◽  
Competitive Protein Binding ◽  
Hypothyroid Patients

ABSTRACT Serum thyroxine concentrations were determined in 66 euthyroid, 30 hyperthyroid and 13 hypothyroid patients using both the established Murphy method and a simplified method of competitive protein binding analysis. A diagnosis compatibility of 96% was found with both methods indicating that the simplified method has comparable clinical application as an initial screen of thyroid status.

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