ASP53, a thermostable protein from Acacia erioloba seeds that protects target proteins against thermal denaturation.
| dc.contributor.author | Mtwisha, Linda | |
| dc.contributor.author | Farrant, Jill M | |
| dc.contributor.author | Brandt, Wolf | |
| dc.contributor.author | Hlongwane, Caswell | |
| dc.contributor.author | Lindsey, George G | |
| dc.date.accessioned | 2016-07-15T14:17:10Z | |
| dc.date.available | 2016-07-15T14:17:10Z | |
| dc.date.issued | 2007 | |
| dc.date.updated | 2016-07-15T14:15:21Z | |
| dc.description.abstract | ASP53, a 53 kDa heat soluble protein, was identified as the most abundant protein in the mature seeds of Acacia erioloba E.Mey. Immunocytochemistry showed that ASP53 was present in the vacuoles and cell walls of the axes and cotyledons of mature seeds and disappeared coincident with loss of desiccation tolerance. The sequence of the ASP53 transcript was determined and found to be homologous to the double cupin domain-containing vicilin class of seed storage proteins. Mature seeds survived heating to 60◦C and this may be facilitated by the presence of ASP53. Circular dichroism spectroscopy demonstrated that the protein displayed defined secondary structure, which was maintained even at high temperature. ASP53 was found to inhibit all three stages of protein thermal denaturation. ASP53 decreased the rate of loss of alcohol dehydrogenase activity at 55◦C, decreased the rate of temperature-dependent loss of secondary structure of haemoglobin and completely inhibited the temperature-dependent aggregation of egg white protein. | en_ZA |
| dc.identifier | http://dx.doi.org/10.1071/FP06135 | |
| dc.identifier.apacitation | Mtwisha, L., Farrant, J. M., Brandt, W., Hlongwane, C., & Lindsey, G. G. (2007). ASP53, a thermostable protein from Acacia erioloba seeds that protects target proteins against thermal denaturation. <i>Functional Plant Biology</i>, http://hdl.handle.net/11427/20390 | en_ZA |
| dc.identifier.chicagocitation | Mtwisha, Linda, Jill M Farrant, Wolf Brandt, Caswell Hlongwane, and George G Lindsey "ASP53, a thermostable protein from Acacia erioloba seeds that protects target proteins against thermal denaturation." <i>Functional Plant Biology</i> (2007) http://hdl.handle.net/11427/20390 | en_ZA |
| dc.identifier.citation | Mtwisha, L., Farrant, J. M., Brandt, W., Hlongwane, C., & Lindsey, G. G. (2007). ASP53, a thermostable protein from Acacia erioloba seeds that protects target proteins against thermal denaturation. Functional plant biology, 34(2), 139-149. | en_ZA |
| dc.identifier.issn | 1445-4408 | en_ZA |
| dc.identifier.ris | TY - Journal Article AU - Mtwisha, Linda AU - Farrant, Jill M AU - Brandt, Wolf AU - Hlongwane, Caswell AU - Lindsey, George G AB - ASP53, a 53 kDa heat soluble protein, was identified as the most abundant protein in the mature seeds of Acacia erioloba E.Mey. Immunocytochemistry showed that ASP53 was present in the vacuoles and cell walls of the axes and cotyledons of mature seeds and disappeared coincident with loss of desiccation tolerance. The sequence of the ASP53 transcript was determined and found to be homologous to the double cupin domain-containing vicilin class of seed storage proteins. Mature seeds survived heating to 60◦C and this may be facilitated by the presence of ASP53. Circular dichroism spectroscopy demonstrated that the protein displayed defined secondary structure, which was maintained even at high temperature. ASP53 was found to inhibit all three stages of protein thermal denaturation. ASP53 decreased the rate of loss of alcohol dehydrogenase activity at 55◦C, decreased the rate of temperature-dependent loss of secondary structure of haemoglobin and completely inhibited the temperature-dependent aggregation of egg white protein. DA - 2007 DB - OpenUCT DP - University of Cape Town J1 - Functional Plant Biology LK - https://open.uct.ac.za PB - University of Cape Town PY - 2007 SM - 1445-4408 T1 - ASP53, a thermostable protein from Acacia erioloba seeds that protects target proteins against thermal denaturation TI - ASP53, a thermostable protein from Acacia erioloba seeds that protects target proteins against thermal denaturation UR - http://hdl.handle.net/11427/20390 ER - | en_ZA |
| dc.identifier.uri | http://hdl.handle.net/11427/20390 | |
| dc.identifier.uri | http://www.publish.csiro.au/?paper=FP06135 | |
| dc.identifier.vancouvercitation | Mtwisha L, Farrant JM, Brandt W, Hlongwane C, Lindsey GG. ASP53, a thermostable protein from Acacia erioloba seeds that protects target proteins against thermal denaturation. Functional Plant Biology. 2007; http://hdl.handle.net/11427/20390. | en_ZA |
| dc.language | eng | en_ZA |
| dc.publisher | CSIRO Publishing | en_ZA |
| dc.publisher.institution | University of Cape Town | |
| dc.source | Functional Plant Biology | en_ZA |
| dc.source.uri | http://www.publish.csiro.au/nid/102.htm | |
| dc.subject.other | circular dichroism spectroscopy | |
| dc.subject.other | immunocytochemistry | |
| dc.subject.other | protection of protein conformation | |
| dc.subject.other | seed stora | |
| dc.title | ASP53, a thermostable protein from Acacia erioloba seeds that protects target proteins against thermal denaturation. | en_ZA |
| dc.type | Journal Article | en_ZA |
| uct.type.filetype | Text | |
| uct.type.filetype | Image | |
| uct.type.publication | Research | en_ZA |
| uct.type.resource | Article | en_ZA |