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   <subfield code="a">Structure and function of eukaryotic peptide transporters</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[D. Meredith*, C. A. R. Boyd]</subfield>
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   <subfield code="a">Abstract.: The cotransport of protons and peptides is now recognised as a major route by which dietary nitrogen is absorbed from the intestine, and filtered protein reabsorbed in the kidney. Recently, molecular biology has had a very substantial impact on the study of peptide transport, and here we review the molecular and functional information available within the framework of physiology. To this end we consider not only the mammalian peptide transporters and their tissue distribution and regulation but also those from other species (including Caenorhabditis elegans) which make up the proton-dependent oligopeptide transport superfamily. In addition, understanding the binding requirements for transported substrates may allow future design and targeted tissue delivery of peptide and peptidomimetic drugs. Finally, we aim to highlight some of the less well understood areas of peptide transport, in the hope that it will stimulate further research into this challenging yet exciting topic.</subfield>
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   <subfield code="a">Birkhäuser Verlag Basel,, 2000</subfield>
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   <subfield code="a">Key words. PepT1</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">PepT2</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">epithelia</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">β-lactam antibiotics</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">PTR2</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">oligopeptide transport</subfield>
   <subfield code="2">nationallicence</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">apical membrane</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">basolateral membrane</subfield>
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   <subfield code="a">Meredith*</subfield>
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   <subfield code="u">Department of Biochemistry, University of Bristol, School of Medical Sciences, University Walk, Bristol BS8 1TD (United Kingdom) Fax 44 117 928 8274, e-mail: david.meredith@bristol.ac.uk, GB</subfield>
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   <subfield code="a">Boyd</subfield>
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   <subfield code="u">Department of Human Anatomy and Genetics, University of Oxford, South Parks Road, Oxford, OX1 3QX (United Kingdom), Fax 44 1865 272420, e-mail: richard.boyd@human-anatomy.ox.ac.uk, GB</subfield>
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   <subfield code="a">Meredith*</subfield>
   <subfield code="D">D.</subfield>
   <subfield code="u">Department of Biochemistry, University of Bristol, School of Medical Sciences, University Walk, Bristol BS8 1TD (United Kingdom) Fax 44 117 928 8274, e-mail: david.meredith@bristol.ac.uk, GB</subfield>
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   <subfield code="u">Department of Human Anatomy and Genetics, University of Oxford, South Parks Road, Oxford, OX1 3QX (United Kingdom), Fax 44 1865 272420, e-mail: richard.boyd@human-anatomy.ox.ac.uk, GB</subfield>
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   <subfield code="a">Metadata rights reserved</subfield>
   <subfield code="b">Springer special CC-BY-NC licence</subfield>
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