INTERSTITIAL ALBUMIN††This research work was supported by Grant HE-02262 from the National Institutes of Health, U.S. Public Health Service, Bethesda, Maryland, and Grant RR-00051, General Clinical Research Center and Colorado Heart Association.

Allergic reactions to the widely applied urinary tract disinfectant nitrofurantoin (NFT) often concern the skin. They are probably mediated by a NFT-protein adduct. which has been suggested to result from incomplete nitro-reduction during metabolism. In this study it was investigated whether photoactivation of NFT in rats, upon exposure to UV-A, leads to formation of adducts between the drug and biomacromolecules. Rats were given p.0. doses of [14CI-NFT, and some were exposed to UV-A. More irreversible binding was found in skin of the back (both in dermis and in epidermis). tail, ears, eyes, plasma proteins. and spleen of light-exposed rats compared to those kept in the dark. This photobinding increased (up to -0.6 nmolimg protein = -25 nmolig tissue) with dose and lightintensity. When rats were kept at 32"C, instead of 22°C during NFTIUV-A treatment. even more irreversible binding was observed; this is probably caused by an increased dermal blood flow. Under these conditions, irreversibly bound radioactivity was even found in kidney. lung and liver. Irreversible binding in these inner organs is explained by systemic distribution of radioactivity. photobound to plasma proteins. Photodecomposition of NFT in the skin, followed by reaction of photoproducts with (cellular) biomacromolecules may explain some of the skin rashes and other (allergic) reactions reported for this drug.

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Tissue Distribution of Ampicillin: Assays in Muscle Tissue and Subcutaneous Tissue Cage Fluid from Normal and Nephrectomized Rabbits

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1981

Scandinavian Journal of Infectious Diseases

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Tissue distribution of ampicillin following a single intravenous injection was studied in normal and functionally nephrectomized rabbits. Serum concentrations of ampicillin were compared with those obtained in subcutaneous tissue cage fluid, muscle (measured by a direct agar diffusion method) and muscle tissue fluid (obtained from implanted cotton threads). Considerable differences were found. Penetration of ampicillin into rabbit muscle was rapid and the elimination half-life was similar to that of serum. Concentrations in tissue cage fluid were low as compared with muscle tissue fluid levels, and penetration and elimination was slower. Results from experiments in functionally nephrectomized rabbits showed that a steady state between serum and muscle seemed to be attained after 15-30 min. These results were used to estimate the degree of protein binding of ampicillin in muscle tissue fluid.

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INTERSTITIAL ALBUMIN††This research work was supported by Grant HE-02262 from the National Institutes of Health, U.S. Public Health Service, Bethesda, Maryland, and Grant RR-00051, General Clinical Research Center and Colorado Heart Association.

Cited by 5 publications

References 60 publications

Humanalbumin: Depot- und/oder Transportprotein für Pharmaka

Humanalbumin: Depot- und/oder Transportprotein für Pharmaka

Irreversible Binding of Nitrofurantoin to Skin and to Plasma Proteins of Uv‐a Exposed Rats

Tissue Distribution of Ampicillin: Assays in Muscle Tissue and Subcutaneous Tissue Cage Fluid from Normal and Nephrectomized Rabbits

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