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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

Bibliography: pages 229-241.

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Main Author: Teixeira, Avelino V
Other Authors: Botes, Dawie
Format: Thesis
Language:English
Published: Department of Molecular and Cell Biology 2016
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access_status_str Open Access
author Teixeira, Avelino V
author2 Botes, Dawie
author_browse Botes, Dawie
Teixeira, Avelino V
author_facet Botes, Dawie
Teixeira, Avelino V
author_sort Teixeira, Avelino V
collection Thesis
description Bibliography: pages 229-241.
format Thesis
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institution University of Cape Town (South Africa)
language eng
last_indexed 2026-06-10T12:32:21.936Z
license_str Not specified — see source repository
provenance_str_mv Harvested via OAI-PMH from UCTD — University of Cape Town Open Access Repository
publishDate 2016
publishDateRange 2016
publishDateSort 2016
publisher Department of Molecular and Cell Biology
publisherStr Department of Molecular and Cell Biology
record_format dspace
source_str UCTD — University of Cape Town Open Access Repository
spelling oai:open.uct.ac.za:11427/21985 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 Teixeira, Avelino V Botes, Dawie Biochemistry Bibliography: pages 229-241. 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. 2016-09-28T19:05:30Z 2016-09-28T19:05:30Z 1992 Doctoral Thesis Doctoral PhD http://hdl.handle.net/11427/21985 eng application/pdf Department of Molecular and Cell Biology Faculty of Science University of Cape Town
spellingShingle Biochemistry
Teixeira, Avelino V
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_degree_str Doctoral
title 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
title_full 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
title_fullStr 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
title_full_unstemmed 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
title_short 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
title_sort 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
topic Biochemistry
url http://hdl.handle.net/11427/21985
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