published_or_final_version / abstract / toc / Biochemistry / Doctoral / Doctor of Philosophy

Thesis (Ph.D.) --Murdoch University, 2003. / Thesis submitted to the Division of Veterinary and Biomedical Sciences. Includes bibliographical references (leaves 160-196).

Thesis (M.S.)--Rochester Institute of Technology, 1991. / Spine title: Active site configuration of GDH. Typescript. References: leaves 73-75.

Thesis (Ph. D.)--University of Washington, 2004. / Vita. Includes bibliographical references (leaves 210-219).

Thesis (Ph. D.)--University of Hong Kong, 1994. / Includes bibliographical references (leaves 72-104).

Thesis (Ph. D.)--University of Hong Kong, 1994. / Includes bibliographical references (leaves 79-105).

Thesis (Ph. D.)--University of Hong Kong, 1994. / Includes bibliographical references (leaves 152-165).

Thesis (Ph. D.)--University of Oregon, 2006. / Typescript. Includes vita and abstract. Includes bibliographical references (leaves 115 - 121). Also available for download via the World Wide Web; free to University of Oregon users.

Restriction enzyme inhibition and lambda exonuclease studies indicate that carcinogen N-acetoxy-N-acetyl-2 aminofluorene (AAAF) binds to sequences on ɸX174 RF and SV40 plasmids DNA that are similar to the eight preferred binding sites previously located on pBR 322. Both DNAs were digested with enzyme Hinf I and resultant fragments 32P end-labeled. Labeled fragments were reacted with the carcinogen to give one to sixteen bound moieties per DNA. Fragments were isolated and restriccion enzyme and lambda exonuclease inhibition assays were performed. Inhibition detected occurred at selected sites and was not specific for a certain enzyme or certain size of recognition sequence. Results of these assays allow mapping of the location of high affinity binding sites of the carcinogen on both DNAs. All sites have common sequence elements: the presence of either the sequence T(G/C)TT(G/C) or the sequence T(G/C) CTT(G/C).

Hemerythrin is a respiratory protein found in the erythrocytes of certain marine invertebrates. Structures have been obtained by x-ray crystallography for hemerythrins from Phascolopsis gouldii (P. gouldii) and Themiste dyscritum (T. dyscritum). Since many proteins are inactivated upon binding heavy metals such as mercury, an investigation of mercury-protein interactions in this protein was undertaken. In order to understand the nature of heavy-metal protein interactions in T. dyscritum it was necessary to identify the metalloprotein ligands since neither the liganding amino acid residues nor the geometry of the mercury complexes could be identified in the crystallographic studies.