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Poly(A)+ RNA From Sheep Omasal Epithelium Induces Expression of a peptide Transport Protein(S) in Xenopus laevis Oocytes

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dc.contributor.authorPan, YuanXiangen
dc.contributor.committeecochairWebb, Kenneth E. Jr.en
dc.contributor.committeecochairWong, Eric A.en
dc.contributor.committeememberBloomquist, Jeffrey R.en
dc.contributor.committeememberHerbein, Joseph H. Jr.en
dc.contributor.departmentAnimal and Poultry Sciencesen
dc.date.accessioned2014-03-14T20:51:24Zen
dc.date.adate1996-08-09en
dc.date.available2014-03-14T20:51:24Zen
dc.date.issued1996-08-09en
dc.date.rdate1996-08-09en
dc.date.sdate1998-07-20en
dc.description.abstractIn order to verify the research from this laboratory that sheep omasal epithelium contains mRNA encoding for a peptide transporter (s) and to determine di- to octapeptide transport capability, poly(A)+ RNA isolated from sheep omasal epithelium was injected into Xenopus laevis oocytes. Poly(A)+ RNA was functionally expressed in Xenopus oocytes 4 to 7 d post-injection. Peptide (5 di-, 10 tri-, 6 tetra-, 2 penta-, 1 hepta-, 1 septa-, 1 octapeptide) transport capability was measured by impaling oocytes with a microelectrode to monitor membrane potential (Vm). Oocytes were maintained in pH 5.5 buffer. Peptide transport was identified as being expressed when, in the presence of a buffered peptide substrate (1 mM), the oocyte membrane showed persistent depolarization (a more positive Vm). In the absence of peptide transport, the membrane became depolarized with the addition of buffered substrate, but rapidly repolarized to the resting potential. Peptide transport was expressed for some di-, tri-, and tetrapeptides. Measured depolarization ranged from 9.6 mV to 42.1 mV. Larger peptides were not transported by the oocytes. When transport expression was measured with the substrates in a pH 7.5 buffer, no transport occurred indicating that transport was dependent on a proton gradient. The data indicate that sheep omasal epithelium contains mRNA that code for a protein(s) capable of proton-dependent di-, tri-, and tetrapeptide transport. This provides further evidence that absorption of peptides from the ruminant stomach is possible.en
dc.description.degreeMaster of Scienceen
dc.identifier.otheretd-3856112379652351en
dc.identifier.sourceurlhttp://scholar.lib.vt.edu/theses/available/etd-3856112379652351/en
dc.identifier.urihttp://hdl.handle.net/10919/36658en
dc.publisherVirginia Techen
dc.relation.haspartpan_thesis.pdfen
dc.relation.haspartetd.pdfen
dc.rightsIn Copyrighten
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subjectsheepen
dc.subjectomasumen
dc.subjectpeptideen
dc.subjecttransporten
dc.subjectelectrophysiologyen
dc.titlePoly(A)+ RNA From Sheep Omasal Epithelium Induces Expression of a peptide Transport Protein(S) in Xenopus laevis Oocytesen
dc.typeThesisen
thesis.degree.disciplineAnimal and Poultry Sciencesen
thesis.degree.grantorVirginia Polytechnic Institute and State Universityen
thesis.degree.levelmastersen
thesis.degree.nameMaster of Scienceen

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