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- W2071492904 abstract "The methylotrophic yeastPichia pastoriswas used for heterologous expression of the rabbit intestinal peptide transporter PepT1 and its functional characterization. PepT1 mediates the electrogenic transmembrane transport of di- and tripeptides and peptido-mimetics such as β-lactam antibiotics and ACEinhibitors. Functional expression of PepT1 was determined in different recombinant clones by flux studies employing the radiolabeled dipeptide3H-(D)-Phe-(L)-Ala. One clone (GS-PepT1) displayed high level functional expression that was pH dependent and saturable with an app. K0.5of 1.17 ± 0.18 mM. Inhibition of3H-(D)-Phe-(L)-Ala uptake into GS-PepT1 by selected dipeptides, tripeptides and peptidomimetics including β-lactam antibiotics and ACE-inhibitors revealed the same substrate specifity as reported for PepT1 when expressed in mammalian cells orXenopus laevisoocytes.Pichiacells expressing PepT1 will provide an excellent tool for in vitro bioavailability studies for peptides and peptidomimetics. Moreover, to our knowledge, this is the first demonstration of functional expression of a mammalian membrane transport protein usingP. pastoris." @default.
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- W2071492904 date "1997-03-01" @default.
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- W2071492904 title "Expression and Functional Characterization of the Mammalian Intestinal Peptide Transporter PepT1 in the Methylotropic YeastPichia pastoris" @default.
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- W2071492904 doi "https://doi.org/10.1006/bbrc.1997.6351" @default.
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