S
Sabina Passamonti
Researcher at University of Trieste
Publications - 132
Citations - 4021
Sabina Passamonti is an academic researcher from University of Trieste. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 31, co-authored 111 publications receiving 3504 citations. Previous affiliations of Sabina Passamonti include University of Padua & National University of Rosario.
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Journal ArticleDOI
Bilitranslocase localization and function in basolateral plasma membrane of renal proximal tubule in rat.
M. M. Elias,Giancarlo Lunazzi,Sabina Passamonti,Bruno Gazzin,Maddalena Miccio,Giorgio Stanta,Gian Luigi Sottocasa,Claudio Tiribelli +7 more
TL;DR: It is concluded that BTL is present in basolateral plasma membrane of RPT cells, and lower affinity of renal, compared with hepatic protein, for substrates might explain the marginal role of kidney in plasma clearance of bilirubin and cholephilic dyes.
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Application of high-performance liquid chromatography combined with ultra-sensitive thermal lens spectrometric detection for simultaneous biliverdin and bilirubin assessment at trace levels in human serum
TL;DR: The concentration ratio of free bilirubin versus unbound biliverdin in human serum samples is shown for the first time, and the applicability of a new ultra-sensitive analytical method is presented.
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The fate of trans-caftaric acid administered into the rat stomach
Andreja Vanzo,Roberto Cecotti,U. Vrhovsek,Adriana M. Torres,Fulvio Mattivi,Sabina Passamonti +5 more
TL;DR: Investigation of trans-caftaric acid absorption, tissue distribution, and metabolism in rats found that the stomach is a relevant site of absorption of dietary polyphenols.
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Specific sequence-directed anti-bilitranslocase antibodies as a tool to detect potentially bilirubin-binding proteins in different tissues of the rat
TL;DR: In the rat, positive proteins bands were found to be present only in the liver, gastric mucosa and central nervous system, and peptides containing the bilirubin‐binding motif identified in bilitranslocase were searched for.
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The quinoid structure is the molecular requirement for recognition of phthaleins by the organic anion carrier at the sinusoidal plasma membrane level in the liver
TL;DR: It is concluded that the phthalein structure recognized for transport is the quinoid molecule, with the dissociated acidic function on the benzene ring, and inhibitions by rifamycin-SV and bilirubin suggest that there exists a common uptake system for bilirubs, phthalesins and other anions.