caa a22 4500 477058027 CHVBK 20180405111352.0 cr unu---uuuuu 170330e19960101xx s 000 0 eng 10.1007/BF00226331 doi (NATIONALLICENCE)springer-10.1007/BF00226331 Interindividual variability in the rate of salbutamol sulphation in the human lung [Elektronische Daten] [G. Pacifici, C. De Santi, A. Mussi, C. Ageletti] The β2-adrenergic agonist salbutamol is administered by inhalation to treat lung-obstructive disease. Salbutamol is metabolized by conjugation with sulphate, and the sulphation of salbutamol was investigated in human lung. Specimens of lung were obtained at lobectomy from 11 non-smokers, 39 smokers and 46 ex-smokers, the latter refraining from smoking at least 6 months before surgery. Neither sex nor ageing influenced the activity of sulphotransferase. The rate of salbutamol sulphation (pmol·min-1·mg-1) was greater in non-smokers (27.7) than in smokers (21.3), whereas it was similar in smoker and ex-smokers (22.8). The rate of salbutamol sulphation ranged up to six fold and its distribution did not deviate from normality. As the rate of formation of the inactive salbutamol sulphate varied in the lung, the availability of salbutamol and, in turn, the evoked pharmacological effect should vary in parallel. The activities of salbutamol and dopamine sulphotransferase correlated, suggesting that catechol sulphotransferase takes part in the sulphation of salbutamol. The sulphation of salbutamol is stereoselective in the human lung, the k M estimate for (+)-salbutamol (1198 μM) being greater than those for either (-)-salbutamol (190 μM) and racemic salbutamol (142 μM). These results are consistent with the view that (-)-salbutamol is a better substrate than (+)-salbutamol for sulphotransferase. Springer-Verlag, 1996 Salbutamol nationallicence lung nationallicence sulphotransferase nationallicence variability nationallicence chirality nationallicence Pacifici G. Department of Biomedicine, Medical School, Via Roma 55, I-56126, Pisa, Italy aut De Santi C. Department of Biomedicine, Medical School, Via Roma 55, I-56126, Pisa, Italy aut Mussi A. Department of Surgery, Medical School, Via Roma 55, I-56126, Pisa, Italy aut Ageletti C. Department of Surgery, Medical School, Via Roma 55, I-56126, Pisa, Italy aut European Journal of Clinical Pharmacology Springer-Verlag 49/4(1996-01-01), 299-303 0031-6970 49:4<299 1996 49 228 https://doi.org/10.1007/BF00226331 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00226331 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Pacifici G. Department of Biomedicine, Medical School, Via Roma 55, I-56126, Pisa, Italy aut NATIONALLICENCE 700 1- De Santi C. Department of Biomedicine, Medical School, Via Roma 55, I-56126, Pisa, Italy aut NATIONALLICENCE 700 1- Mussi A. Department of Surgery, Medical School, Via Roma 55, I-56126, Pisa, Italy aut NATIONALLICENCE 700 1- Ageletti C. Department of Surgery, Medical School, Via Roma 55, I-56126, Pisa, Italy aut NATIONALLICENCE 773 0- European Journal of Clinical Pharmacology Springer-Verlag 49/4(1996-01-01), 299-303 0031-6970 49:4<299 1996 49 228 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer