RESUMEN
An animal model of the Long-Evans species of rats was developed to study the short-term and long-term effects of enterocystoplasty. Various enterocystoplasties were performed in 39 rats, including ileal in 29, colonic in 5 and gastric in 5. The followup period was 3 months. Frequency and pattern of voiding, 24-hour urinary collection for mucus production, and blood and urinary electrolytes were analyzed. All voiding parameters, renal function and biochemical studies remained normal. Mucus production was higher in the gastrocystoplasty and colocystoplasty than in ileocystoplasty cases. Postmortem histopathological examination of the enteropatch was performed, which showed urothelialization of the graft with native transitional epithelium extending over the junctional margin of the graft and covering the enteropatch mucosa. The enteropatch muscle orientation was maintained in all 3 types of grafts. We believe that the Long-Evans species of rats is a good model for the study of enterocystoplasty.
Asunto(s)
Vejiga Urinaria/cirugía , Animales , Electrólitos/sangre , Electrólitos/orina , Femenino , Humanos , Intestinos/trasplante , Riñón/patología , Moco/metabolismo , Ácido N-Acetilneuramínico , Ratas , Ácidos Siálicos/orina , Vejiga Urinaria/metabolismo , Vejiga Urinaria/patología , Micción , OrinaRESUMEN
An enzyme immunoassay technique (EMIT) for microdeterminations of caffeine was compared with high performance liquid chromatography (HPLC) and evaluated in 113 neonates and young infants, and in 18 asthmatic and 15 epileptic children. The EMIT assay was found reliable in therapeutic drug monitoring. It offers advantages over HPLC in its rapidity and simplicity. It is not affected by hemolysis, hyperbilirubinemia, or lipemia. In the neonate, greater accuracy is obtained with blood samples containing no heparin.
Asunto(s)
Cafeína/sangre , Síndromes de la Apnea del Sueño/sangre , Anticoagulantes/uso terapéutico , Asma/tratamiento farmacológico , Cafeína/uso terapéutico , Cromatografía Líquida de Alta Presión , Humanos , Técnicas para Inmunoenzimas , Indicadores y Reactivos , Lactante , Recién Nacido , Monitoreo FisiológicoRESUMEN
In vitro binding studies have shown that warfarin binds strongly to both ligandins (Y) and Z protein obtained from rat liver cytosol with dissociation constants of 11.7 and 10.1 microM respectively. Increasing concentrations of oleate ion significantly increased the dissociation constant of warfarin with either protein, whereas laurate ion showed the same behavior only with Z protein. On the other hand, the binding of warfarin to liver cytoplasmic proteins in vivo was decreased in 72-h-pre-fasted rats, although such fasting failed to produce any increase in the in vivo levels of the cytoplasmic free fatty acids (FFA). However, based on the results of the in vitro binding study, it is suggested that changes in the composition of hepatic cytoplasmic free fatty acids as a result of fasting could reduce the in vivo binding of warfarin to Y and Z proteins and hence could lead to an increase of unbound warfarin in liver cytosol.
Asunto(s)
Ácidos Grasos no Esterificados/farmacología , Hígado/metabolismo , Proteínas/metabolismo , Warfarina/metabolismo , Animales , Citoplasma/metabolismo , Ayuno , Glutatión Transferasa/metabolismo , Técnicas In Vitro , Lauratos/farmacología , Masculino , Ácidos Oléicos/farmacología , Unión Proteica/efectos de los fármacos , Ratas , Sulfobromoftaleína/metabolismoRESUMEN
The influence of oleate ion, a free fatty acid anion, on the binding characteristics of 1-anilino-8-naphthalene sulfonate (ANS) with the cytoplasmic proteins (Y and Z) from rat liver has been examined using fluorescence spectroscopy. ANS binds strongly with both ligandin (Y) and Z protein at a single binding site with dissociation constants of 0.6 and 1.4 micron respectively. Increasing concentrations of oleate ion decreased the ANS binding with either protein by competing with the ANS binding site. Relative binding constant of oleate ion for the hepatic ligandin or Z protein was about 2 micron as determined from the competitive inhibition of ANS binding. These results suggest that variations in the hepatic cytoplasmic free fatty acid concentration may be important in regulating the capacity of Y and Z proteins to transport other organic anions.
Asunto(s)
Naftalenosulfonatos de Anilina/metabolismo , Ácidos Grasos no Esterificados/farmacología , Hígado/metabolismo , Animales , Sitios de Unión , Citoplasma/efectos de los fármacos , Citoplasma/metabolismo , Técnicas In Vitro , Hígado/efectos de los fármacos , Masculino , Ácidos Oléicos/farmacología , Unión Proteica/efectos de los fármacos , Conformación Proteica , Ratas , Espectrometría de FluorescenciaRESUMEN
The binding in vitro of tritiated aldosterone to domestic duck (Anas platyrhynchos) kidney tissue has been investigated. Using tissue from animals on a normal diet, tritiated aldosterone was specifically bound to kidney cytosol with an apparent equilibrium dissociation constant of about 9 nM and number of binding sites in the 20 fmol/mg protein range. These values did not show statistically significant changes when the cytosol originated from animals with salt activated nasal glands. Kidney cytosols labeled with tritiated aldosterone sedimented with a single peak at 8S in a linear sucrose gradient (10--30%) and this peak was quenched by excess, radioinert aldosterone. Following incubation of labeled cytosols with crude nuclei, the cytosols became depleted of the label and aldosterone was translocated to the Tris-soluble and Tris-insoluble, 0.4 M KC1 soluble nuclear fractions. Kidney cytosols metabolized aldosterone extensively to a compound presumed to be 3alpha,5beta-tetrahydroaldosterone. However, only unchanged aldosterone became receptor-bound. It was concluded that the duck kidney possesses aldosterone receptors, though competition studies indicated that the specificity of these receptors might be different from those described in the mammalian kidney.