dc.contributor.author |
Goodchild, Bruce |
|
dc.date.accessioned |
2009-04-14T22:02:47Z |
|
dc.date.accessioned |
2022-10-20T11:03:39Z |
|
dc.date.available |
2009-04-14T22:02:47Z |
|
dc.date.available |
2022-10-20T11:03:39Z |
|
dc.date.copyright |
1968 |
|
dc.date.issued |
1968 |
|
dc.identifier.uri |
https://ir.wgtn.ac.nz/handle/123456789/22281 |
|
dc.description.abstract |
1. Low voltage electrophoresis on cellulose acetate paper, high voltage paper electrophoresis, and density gradient electrophoresis have been applied to glutathione S-aryltransferase and DDT-dehydrochlorinase.
2. Density gradient electrophoresis was found to be excellent for enzyme separations.
3. Glutathione S-aryltransferase has been shown to be a distinct enzyme from DDT-dehydrochlorinase in the housefly, Musca domestica.
4. Both male and female houseflies appear to possess two distinct DDT-dehydrochlorinases.
5. Isoelectric points have been found for grass grub (Costelytra zealandica) and housefly glutathione S-aryltransferases and for both housefly DDT-dehydrochlorinases.
6. Electrophoretic mobilities have been calculated for housefly glutathione S-aryltransferase and DDT-dehydrochlorinases.
7 .pH stability curves have been plotted for the fly enzymes.
8. The molecular weights of the fly enzymes have been determined by gel filtration. |
en_NZ |
dc.format |
pdf |
en_NZ |
dc.language |
en_NZ |
|
dc.language.iso |
en_NZ |
|
dc.publisher |
Te Herenga Waka—Victoria University of Wellington |
en_NZ |
dc.title |
Electrophoretic and Stability Studies on Glutathione S-Aryltransferase and DDT Dehydrochlorinase |
en_NZ |
dc.type |
Text |
en_NZ |
vuwschema.type.vuw |
Awarded Research Masters Thesis |
en_NZ |
thesis.degree.discipline |
Biochemistry |
en_NZ |
thesis.degree.grantor |
Te Herenga Waka—Victoria University of Wellington |
en_NZ |
thesis.degree.level |
Masters |
en_NZ |
thesis.degree.name |
Master of Science |
en_NZ |