Thesis (Ph. D.)--University of Chicago, Dept. of Statistics, August 2001. / Includes bibliographical references. Also available on the Internet.

published_or_final_version / Medicine / Master / Master of Research in Medicine

published_or_final_version / Medicine / Master / Master of Research in Medicine

published_or_final_version / Dentistry / Doctoral / Doctor of Philosophy

published_or_final_version / Clinical Oncology / Master / Master of Philosophy

published_or_final_version / abstract / toc / Zoology / Master / Master of Philosophy

No description available.

The gene encoding chicken growth hormone (GH) was isolated from a chicken genomic library. The size of the gene was 4 kb. It was digested with PstI and subcloned into pUC18. Three of the PstI fragments were used for restriction fragment length polymorphisms (RFLPs) analysis at the GH locus in two chicken strains (fat and lean line). Four polymorphic sites were detected using a PstI fragment (PII) as a probe. One polymorphism was located at a SacI restriction site (PS1), and three at MspI sites (PM1, PM2 and PM3). A method based on polymerase chain reaction (PCR) was developed for detecting polymorphisms at PM3 site. A fragment of 823 base pairs which contained the PM3 polymorphic site was amplified. Three genotypes (+/+,$-$/$-$ and +/$-$) were distinguished by examining the MspI digested PCR products in either agarose or polyacrylamide gel. / Ten anonymous cDNA clones were also isolated from a chicken liver cDNA library and used for RFLPs analysis. Three of these clones were found to be able to detected RFLPs at MspI sites in chicken strains (strain 7, 8, 9, 8R, S and K) indicating that a high frequency of genes are polymorphic and can be used as markers in mapping experiments. One of the three clones was present on a haploid genetic element. Segregation analysis showed that the inheritance of this haploid gene was determined by the genotype of the female parent.

No description available.

The human wildtype p53 tumor suppressor gene contains a polymorphism at amino acid residue 72 which results in either an arginine (p53 Arg-72) or proline (p53 Pro-72) at this codon. In the present study I have examined this polymorphism at the molecular level to determine whether differences exist in the biochemical functions of these two p53 variants. No differences were observed in their sequence-specific DNA binding abilities, nor in their ability to be targeted by HPV-18 E6 oncoprotein for degradation by ubiquitination in vitro. However, differences were observed in the ability of these two variants to function as transcriptional activators: p53 Pro-72 was more transcriptionally active than p53 Arg-72. I propose that the polymorphism at codon 72 may affect the structure of the N-terminal transactivation domain of the p53 protein, which would then have an effect on the ability of these variants to interact with transcription factors in order to initiate transcription of target genes and function as a tumor suppressor.