Binding of Some Phenoxyalkanoic Acids to Bovine Serum Albumin &lt;i&gt;in vitro&lt;/i&gt;

Mason, R.W.

doi:10.1159/000136898

Cited by 6 publications

(3 citation statements)

References 5 publications

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“…In contrast, the protein binding of 2,4,5-T was clearly higher and consequently its entry into the brain was lower than either 2,4-D or MCPA. Similar difference between 2,4-D and 2,4,5-T in their binding to bovine serum albumin has been also found (Mason 1975). Our present and earlier studies (EIo andYlitalo 1977, 1979) indicate that at low doses the brain and CSF concentrations of MCPA and 2,4-D in rats are very low but their brain/plasma ratios rise sharply between the doses of 100 and 250 mg/kg.…”

Section: Discussionsupporting

confidence: 73%

“…After gentle shaking of the mixture at 37 ~ C for 1 h, protein-bound and -unbound (free) radioactivity was separated by the Centrifree TM Micropartition System (Amicon Corp., Danvers, MA, USA) which is based on the ultrafiltration, and the radioactivity in each fraction was counted. The ultrafiltration technique has been used earlier to study the binding of 2,4-D, 2,4,5-T and MCPA to bovine serum albumin in vitro (Mason 1975;Koschier et al 1979). The binding of 2,4-D and 2,4,5-T (10 p~M) to the Amicon filter is small (< 15%) (Koschier et al 1979).…”

Section: Methodsmentioning

confidence: 99%

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Distribution of three common chlorophenoxyacetic acid herbicides into the rat brain

1990

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The distribution of three common 14C-labelled chlorophenoxyacetic acid herbicides (2,4-dichlorophenoxyacetic acid or 2,4-D, 2-methyl-4-chlorophenoxyacetic acid or MCPA, 2,4,5-trichlorophenoxyacetic acid or 2,4,5-T) into the different brain areas was studied in rats pretreated with toxic doses of the herbicides (238-475 mg/kg). Also, their binding to proteins in rat plasma was determined in vitro by increasing the concentrations of chlorophenoxyacetic acids in the incubate from 0 to 1 mg/ml. Both 2,4-D and MCPA pretreatments increased brain concentrations of 14C-labelled herbicides more markedly than 2,4,5-T pretreatments did. No essential differences were found in the distribution between the different brain areas. Protein-unbound fractions of 2,4-D and MCPA in the plasma were clearly higher than those of 2,4,5-T but the highest herbicide concentration increased the protein-unbound fraction of 2,4,5-T more (7-13-fold) than of 2,4-D and MCPA (5-fold). The results suggest that the greater increase in the penetration into the brain of 2,4-D and MCPA than of 2,4,5-T during their intoxication is due to some factors other than the changes in their binding to plasma proteins and mere enhanced diffusion through the blood-brain barrier.

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Section: Discussionsupporting

confidence: 73%

Section: Methodsmentioning

confidence: 99%

Distribution of three common chlorophenoxyacetic acid herbicides into the rat brain

1990

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“…Similarly, several examples of drug-protein complex formation involving exten sive van der Waals bonding and accompanied by large negative AH°s have been reported (10). Hydrogen bonding and van der Waals interactions are inconsistent with the observed thermodynamic parameters of the aurothiomalate-BSA inter action.…”

Section: Discussionmentioning

confidence: 98%

The Binding of Aurothiomalate to Plasma Proteins <i>in vitro</i>

Mason¹

1977

Pharmacology

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The physicochemical factors responsible for the aurothiomalate-albumin interaction were studied by a thermodynamic analysis of the binding of the anion to bovine albumin. The binding process was entropically driven and it was concluded that electrostatic bonding formed the basis of the aurothiomalate-albumin interaction. The binding of aurothiomalate to human plasma proteins at 37 °C and pH 7.45 and the modification of its binding by indomethacin and phenylbutazone was studied by ultrafíltration. Aurothiomalate was bound to human plasma albumin at a single site with an affinity constant of 6.1 × 10³M^-1and also at several sites of lower affinity. The plasma protein binding of the anion was increased in the presence of indomethacin and phenylbutazone. At therapeutic concentrations in vitro phenylbutazone significantly increased the plasma protein binding of aurothiomalate.

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In vitro binding of14C-labeled acidic compounds to serum albumin and their tissue distribution in the rat

Fang

Lindstrom

1980

Journal of Pharmacokinetics and Biopharmaceutics

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The acidic compounds, such as phenoxyacetic acids, substituted benzoic acids, or acetylsalicylic acid, were found to bind to bovine serum albumin (BSA). Among phenoxyacetic acids, the binding affinity to BSA was highest for 2,4,5-trichlorophenoxyacetic acid (2,4,5-T), which was approximately 4-, 24-, and 160-fold greater than those for 2,4-dichlorophenoxyacetic acid (2,4-D), o-chlorophenoxyacetic acid (CPA), and phenoxyacetic acid (PAA), respectively. There were two bound to serum albumins of other mammalian species. The binding affinity varied among species and also depended on the chemicals. However, the order of binding affinity in the albumin of each species remained the same as observed in BSA with few exceptions. Blood/tissue ratios of 14C from rats dosed with these 14C-labeled acids were highly correlated with the logarithm of the binding affinity constantsaffinity constants.

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Binding of Some Phenoxyalkanoic Acids to Bovine Serum Albumin <i>in vitro</i>

Cited by 6 publications

References 5 publications

Distribution of three common chlorophenoxyacetic acid herbicides into the rat brain

Distribution of three common chlorophenoxyacetic acid herbicides into the rat brain

The Binding of Aurothiomalate to Plasma Proteins <i>in vitro</i>

In vitro binding of14C-labeled acidic compounds to serum albumin and their tissue distribution in the rat

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