The test - retest reliability coefficients of the values of measurements made on the pH, the Pco₂, the standard bicarbonate, the base excess, and the buffer base, of arterial whole blood were estimated for a group of 30 male subjects with the use of the Astrup Micro-equipment, the Siggaard-Andersen revised Nomogram, and a testing program on three successive mornings. Reliability coefficients were estimated for these parameters in both the resting and the post-exercise conditions, and the intra-indivldual and the inter-individual variances were estimated for each reliability coefficient. It was found that the standard bicarbonate and the base excess had the more reliable values, and that the pH and PC0₂ had less reliable values. It was shown that the values of measurements of pH, standard bicarbonate and base excess were significantly different on Day 1 from those values on Days 2 and 3. This effect was attributed to apprehension towards the testing experience and to the strangeness of the testing environment. The measurement errors of the Astrup Micro-equipment and the Siggaard-Andersen revised Nomogram were estimated for the individual parameters. It was found that the buffer base was the only parameter in which the pH meter measurement error variance was large enough to have a decided effect upon the value of the reliability coefficient. The Nomogram measurement error variances were so small that they could be considered negligible. The temporal measurement error of the collection of blood - the error inherent in the time difference between the collection of successive tubes of blood - was investigated for the pH parameter. This temporal measurement error was shown to be practically negligible although statistically significant in the resting condition, but was shown to have both practical importance and statistical significance in the post-exercise condition. / Education, Faculty of / Curriculum and Pedagogy (EDCP), Department of / Graduate

"May 2002." / Thesis (Ph.D.)--Chinese University of Hong Kong, 2002. / Includes bibliographical references (p. 142-163). / Electronic reproduction. Hong Kong : Chinese University of Hong Kong, [2012] System requirements: Adobe Acrobat Reader. Available via World Wide Web. / Electronic reproduction. Ann Arbor, MI : ProQuest Information and Learning Company, [200-] System requirements: Adobe Acrobat Reader. Available via World Wide Web. / Mode of access: World Wide Web. / Abstracts in English and Chinese.

Thesis (doctoral)--Lund University, 1994. / Added t.p. with thesis statement inserted.

Proefschrift--Utrecht. / Summaries in Dutch and English. "Literatuur": p. [82]-92.

Afhandling - Copenhagen. / English summary. "Litteraturfortegnelse": p. 229-[240].

Thesis (doctoral)--Lund University, 1994. / Added t.p. with thesis statement inserted.

Thesis (doctoral)--Lund University, 1997. / Added t.p. with thesis statement inserted. Incorrect ISBN on t.p. verso.

Thesis (doctoral)--Lund University, 1997. / Added t.p. with thesis statement inserted. Incorrect ISBN on t.p. verso.

Thesis (Ph. D.)--University of Wisconsin--Madison, 1965. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.

The homodimeric hemoglobin (HbI) from the blood clam Scapharca inaequivalvis binds oxygen cooperatively and thus offers a simple model system for studying communication between two chemically identical sites. Although the individual subunits of HbI have the same myoglobin-fold as mammalian hemoglobins, the quaternary assemblage is radically different. Upon oxygen binding by HbI, only small tertiary changes are seen at the subunit interface in contrast to the relatively large quaternary changes observed with mammalian hemoglobins. Analysis of structures of this hemoglobin in the liganded (02or CO) and unliganded states has provided a framework for understanding the role of individual amino acid side-chains in mediating cooperativity. The work presented in this dissertation has directly tested the central tenets of the proposed structural mechanism for cooperativity in HbI, illuminating the key roles played by residue Phe 97 and interface water molecules in intersubunit communication. Heterologous expression of Scapharca dimeric hemoglobin: A synthetic gene has been utilized to express recombinant RbI in Escherichia coli. The HbI apoprotein constitutes 5-10% of the total bacterial protein in this system. Addition of the heme precursor δ-aminolevulinic acid to the expression culture results in a ~3-fold increase in the production of soluble hemoglobin. Recombinant HbI has been successfully purified to homogeneity, resulting in a final yield of 80-100 mg of pure holoprotein from a 12 L expression culture. Analysis of recombinant HbI reveals its oxygen binding properties to be indistinguishable from native HbI. It was necessary to correct a protein sequence error by mutating residue Asn 56 to aspartate in order to obtain diffraction quality crystals, that are isomorphous to native HbI crystals. These recombinant HbI crystals diffract to high resolution, permitting the functional effects of mutant HbI proteins to be correlated with detailed structural analysis.