Thesis (Ph. D.)--University of Chicago, 1915. / Reprinted from the Journal of experimental medicine, vol. XXII, no. 2, 3, 1915. Includes bibliographical references (p. 235, 388). Also available on the Internet.

Thesis (M.S.)--University of Wyoming, 2007. / Title from PDF title page (viewed on June 10, 2009). Includes bibliographical references (p. 66-77).

Proefschrift--Leyden. / "Stellingen" ([2] p.) inserted. Bibliography: p. 101-102.

Thesis (Ph. D.)--University of Pennsylvania, 1937.

Thesis (Ph. D.)--University of Wisconsin--Madison, 1951. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 106-107).

Thesis (Ph. D.)--University of Chicago, 1936. / Lithoprinted. "Private edition, distributed by the University of Chicago libraries, Chicago, Illinois." Includes bibliographical references.

Thesis (Ph. D.)--University of Wisconsin--Madison, 1948. / Vita. Typescript. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaf [36]).

Thesis (M.S.)--University of Wisconsin--Madison, 1970. / eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.

In this thesis reactions of urea and its N-alkyl derivatives with monoketones, α-diketone s, enzladehyde, acyloins, diaminoethane and its N-alkyl derivatives, oxidation of alkyl and aryl derivatives of thiourea, nitration of Hector's Base, effect of bases on the adduct of Hector's Base, structural elucidation of Hector's Base, Dost's Base and related compound by the application of spectral techniques, and the reaction of picric acid with creatinine in alkaline media are discussed. Reactions of monoketones (acetone, mesityl oxide, aceto-phenone and benzophenone) and benzaldehyde with urea, 1-methylurea and 1,3-dimethylurea gave white crystalline product These products were identified by proton and carbon-13 nmr techniques, physical, chemical and spectrophotometric methods wherever appropriate. A mechanism for these reactions has been proposed. In all these cases, monoketones (except benzophenone) undergo self-condensation in acid solution and the resulting products react with ureas. In the absence of ureas there is further self-condensation to yield hydrocarbons. In case of benzaldehyde reaction, it is the urea which undergoes self-condensation and resulting biuret, in turn, reacts with benzaldehyde. Moreover, it has been found that at least one methyl group adjacent to carbonyl group is involved in the self-condensation process. If methyl groups on either side of carbonyl group are replaced by phenyl groups (benzophenone) then there is no reaction.

Monoclonal antibodies (Mabs) raised against Ureaplasma urealyticum (serotype 8) revealed the presence of three membrane antigens. One major surface antigen of apparent molecular mass 96 kDa, shown to express four distinct epitopes, was found to be serotype-8 specific. Thus, Mabs raised against this polypeptide will unequivocally differentiate serotype 8 from the other serotypes of human origin. The binding of antibodies to this polypeptide partially suppressed the growth of the organisms. Membrane expressed antigenic polypeptides of apparent molecular masses 16 kDa and 17 kDa were expressed by those serotypes belonging to the large serocluster (A), whereas the 17 kDa polypeptide only was expressed in the smaller serocluster (B). Using this Mab probe serotype 13 was placed in the larger serocluster. Thus Mabs, which recognise one or both of these polypeptides, will unequivocally differentiate the two seroclusters of this organism. The cytosolic urease from U. urealyticum, serotype 8, was purified by immuno-affinity chromatography. Two active forms of the enzyme were demonstrated by non-denaturing electrophoretic analysis and a single peak with urease activity of apparent molecular mass 190 KDa was shown by FPLC. Freezing and thawing of the purified enzyme caused a partial breakdown to inactive sub-units whereas total inactivation of the enzyme and denaturation, achieved by boiling for two minutes in the absence of any added denaturing agents, revealed three subunit polypeptides of apparent molecular masses 72, 14 and 11 KDa. Densitometry suggested that the active enzyme contains equimolar ratios of the three subunits and hence is a hexamer. The active enzyme displayed two pH optima of 6.9 and 6.15. Mabs raised against purified urease bound to both the active enzyme and to the inactive 72 kDa subunit. No evidence of antigenicity was found for the 14 and 11 KDa sub-units. These Mabs cross-reacted with ureases from all the other human serotypes. Competition assays revealed a minimum of four and possibly five distinct epitopes on the enzyme, all distinct from its active site. Ureaplasmas from 5 animal hosts were studied using the various Mabs. The 96 kDa antigen was not found in any of the non-human strains. Variations in the available epitopes on the ureases and the presence or absence of the 16/17 KDa antigens in the non-human strains allowed a putative identification of the source of the non-human ureaplasmas. Such investigations also showed that with the exception of the 96 KDa serotype 8-specific antigen, chimpanzee isolates could not be differentiated from the human ureaplasma serotypes belonging to the large serocluster. These Mabs were also used to develop fluorescent probes and other diagnostic assays which included a slide agglutination system and a sensitive urease catch assay which was also converted into a 'dip-stick' assay.