An L-amino acid oxidase is extracted from whole Neurospora crassa conidia when they are treated with saturated (4.8 M) KCL. This procedure preferentially extracts cell surface molecules, many of which are components of the amino acid transport system and leaves the cells completely viable. / The L-amino acid oxidase has a molecular weight of 160,000 daltons by gel filtration chromatograhy and 85,000 daltons by SDS polyacrylamide gel electrophoresis. The oxidase is sensitive to zinc ions, and not to the sulfhydryl reagent, iodoacetic acid. The neutral (N) amino acid transport system in Neurospora crassa is also sensitive to zinc ions. The similarity between the concentration dependence of zinc inhibition of the oxidase and the transport system suggests that the oxidase may be involved in the membrane-mediated transport process. / Source: Dissertation Abstracts International, Volume: 41-11, Section: B, page: 4003. / Thesis (Ph.D.)--The Florida State University, 1980.
| Identifer | oai:union.ndltd.org:fsu.edu/oai:fsu.digital.flvc.org:fsu_74360 |
| Contributors | COLLIER, IVAN ELLSWORTH., Florida State University |
| Source Sets | Florida State University |
| Detected Language | English |
| Type | Text |
| Format | 188 p. |
| Rights | On campus use only. |
| Relation | Dissertation Abstracts International |
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