Synthesis and expression of the Erythrina trypsin/tissue plasminogen activator (tPA) inhibitor encoding-gene : genetic dissection to correlate the interaction of Erythrina and Soybean trypsin inhibitors with tPA

Simple item page
dc.contributor.advisorBotes, Dawieen_ZA
dc.contributor.authorTeixeira, Avelino Ven_ZA
dc.date.accessioned2016-09-28T19:05:30Z
dc.date.available2016-09-28T19:05:30Z
dc.date.issued1992en_ZA
dc.descriptionBibliography: pages 229-241.en_ZA
dc.description.abstractA trypsin inhibitor had previously been isolated from Erythrina caffra, a member of the Leguminosae family. The inhibitor, Erythrina trypsin inhibitor (ETI), is unique among plantderived inhibitors, in that in addition to trypsin, it inhibits chymotrypsin and tissue plasminogen activator (tPA). ETI was previously sequenced and its crystal structure determined from which it could be seen that ETI has good homology to soybean trypsin inhibitor (STI). However, STI does not inhibit tPA. From the three-dimensional structure of ETI it was known that the amino-terminus of the molecule forms a finger-like structure stabilized by hydrogen bonds and hydrophobic interactions. In addition, the N-terminal finger region is located in close proximity to the reactive site loop and the Nterminal residue (Val) is bound up in the finger region. In STI the N-terminal region is located in close proximity to the reactive site loop and is folded into a structure similar to that in ETI. While the crystal structure of STI was not detailed enough to determine secondary interactions such as hydrogen bonds it was hypothesized that the N-terminal region is stabilized as in ETI. It was further hypothesized that the N-terminal residue of STI (Asp), because of its hydrophilic nature, is not involved in the structured N-terminal finger region of this protein. This leaves this Asp residue of STI free to form an ion pair with Lys at position 60 in trypsin when STI and trypsin interact.en_ZA
dc.identifier.apacitationTeixeira, A. V. (1992). <i>Synthesis and expression of the Erythrina trypsin/tissue plasminogen activator (tPA) inhibitor encoding-gene : genetic dissection to correlate the interaction of Erythrina and Soybean trypsin inhibitors with tPA</i>. (Thesis). University of Cape Town ,Faculty of Science ,Department of Molecular and Cell Biology. Retrieved from http://hdl.handle.net/11427/21985en_ZA
dc.identifier.chicagocitationTeixeira, Avelino V. <i>"Synthesis and expression of the Erythrina trypsin/tissue plasminogen activator (tPA) inhibitor encoding-gene : genetic dissection to correlate the interaction of Erythrina and Soybean trypsin inhibitors with tPA."</i> Thesis., University of Cape Town ,Faculty of Science ,Department of Molecular and Cell Biology, 1992. http://hdl.handle.net/11427/21985en_ZA
dc.identifier.citationTeixeira, A. 1992. Synthesis and expression of the Erythrina trypsin/tissue plasminogen activator (tPA) inhibitor encoding-gene : genetic dissection to correlate the interaction of Erythrina and Soybean trypsin inhibitors with tPA. University of Cape Town.en_ZA
dc.identifier.ris TY - Thesis / Dissertation AU - Teixeira, Avelino V AB - A trypsin inhibitor had previously been isolated from Erythrina caffra, a member of the Leguminosae family. The inhibitor, Erythrina trypsin inhibitor (ETI), is unique among plantderived inhibitors, in that in addition to trypsin, it inhibits chymotrypsin and tissue plasminogen activator (tPA). ETI was previously sequenced and its crystal structure determined from which it could be seen that ETI has good homology to soybean trypsin inhibitor (STI). However, STI does not inhibit tPA. From the three-dimensional structure of ETI it was known that the amino-terminus of the molecule forms a finger-like structure stabilized by hydrogen bonds and hydrophobic interactions. In addition, the N-terminal finger region is located in close proximity to the reactive site loop and the Nterminal residue (Val) is bound up in the finger region. In STI the N-terminal region is located in close proximity to the reactive site loop and is folded into a structure similar to that in ETI. While the crystal structure of STI was not detailed enough to determine secondary interactions such as hydrogen bonds it was hypothesized that the N-terminal region is stabilized as in ETI. It was further hypothesized that the N-terminal residue of STI (Asp), because of its hydrophilic nature, is not involved in the structured N-terminal finger region of this protein. This leaves this Asp residue of STI free to form an ion pair with Lys at position 60 in trypsin when STI and trypsin interact. DA - 1992 DB - OpenUCT DP - University of Cape Town LK - https://open.uct.ac.za PB - University of Cape Town PY - 1992 T1 - Synthesis and expression of the Erythrina trypsin/tissue plasminogen activator (tPA) inhibitor encoding-gene : genetic dissection to correlate the interaction of Erythrina and Soybean trypsin inhibitors with tPA TI - Synthesis and expression of the Erythrina trypsin/tissue plasminogen activator (tPA) inhibitor encoding-gene : genetic dissection to correlate the interaction of Erythrina and Soybean trypsin inhibitors with tPA UR - http://hdl.handle.net/11427/21985 ER - en_ZA
dc.identifier.urihttp://hdl.handle.net/11427/21985
dc.identifier.vancouvercitationTeixeira AV. Synthesis and expression of the Erythrina trypsin/tissue plasminogen activator (tPA) inhibitor encoding-gene : genetic dissection to correlate the interaction of Erythrina and Soybean trypsin inhibitors with tPA. [Thesis]. University of Cape Town ,Faculty of Science ,Department of Molecular and Cell Biology, 1992 [cited yyyy month dd]. Available from: http://hdl.handle.net/11427/21985en_ZA
dc.language.isoengen_ZA
dc.publisher.departmentDepartment of Molecular and Cell Biologyen_ZA
dc.publisher.facultyFaculty of Scienceen_ZA
dc.publisher.institutionUniversity of Cape Town
dc.subject.otherBiochemistryen_ZA
dc.titleSynthesis and expression of the Erythrina trypsin/tissue plasminogen activator (tPA) inhibitor encoding-gene : genetic dissection to correlate the interaction of Erythrina and Soybean trypsin inhibitors with tPAen_ZA
dc.typeDoctoral Thesis
dc.type.qualificationlevelDoctoral
dc.type.qualificationnamePhDen_ZA
uct.type.filetypeText
uct.type.filetypeImage
uct.type.publicationResearchen_ZA
uct.type.resourceThesisen_ZA
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
thesis_sci_1992_teixeira_avelino_v.pdf
Size:
3.41 MB
Format:
Adobe Portable Document Format
Description:
Download
Collections
PhD / Doctoral