Thesis (Ph. D.)--University of Wisconsin--Madison, 1959. / Typescript. Abstracted in Dissertation abstracts, v. 20 (1959) no. 3, p. 895. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 101-104).

Yeung, Ching Yee. / Thesis (M.Phil.)--Chinese University of Hong Kong, 2008. / Includes bibliographical references (leaves 112-122). / Abstracts in English and Chinese. / Acknowledgments --- p.I / Abstract --- p.II / 摘要 --- p.III / Content --- p.IV / Abbreviations and symbols --- p.XI / List of tables and figures --- p.XV / Chapter Chapter 1 --- Introduction --- p.1 / Chapter 1.1 --- Acylphosphatase --- p.1 / Chapter 1.2 --- Human acylphosphatase --- p.4 / Chapter 1.3 --- Hyperthermophilic Pyrococcus horikoshii acylphosphatase --- p.5 / Chapter 1.4 --- Human common-type acylphosphatase as a mesophilic homologue of Pyrococcus horikoshii acylphosphatase --- p.8 / Chapter 1.5 --- Enzyme-substrate interaction of acylphosphatase --- p.9 / Chapter Chapter 2 --- Materials and methods --- p.10 / Chapter 2.1 --- Preparation of Escherichia coli competent cells --- p.10 / Chapter 2.2 --- SDS-polyacrylamide gel electrophoresis --- p.11 / Chapter 2.2.1 --- Preparation of polyacrylamide gel --- p.11 / Chapter 2.2.2 --- SDS-polyacrylamide gel electrophoresis (SDS-PAGE) --- p.12 / Chapter 2.2.3 --- Staining of protein in polyacrylamide gel by Coommassie Brillant Blue R250 --- p.12 / Chapter 2.3 --- Expression and purification of Protein --- p.13 / Chapter 2.3.1 --- "General bacterial culture, harvesting and lysis" --- p.13 / Chapter 2.3.2 --- Purification of acylphosphatase --- p.14 / Chapter 2.3.2.1 --- Ion-exchange chromatography --- p.14 / Chapter 2.3.2.2 --- Size excision chromatography --- p.15 / Chapter 2.3.3 --- Protein concentration determination --- p.16 / Chapter 2.4 --- X-ray crystallography --- p.17 / Chapter 2.4.1 --- Crystallization of Hu CT AcP --- p.17 / Chapter 2.4.2 --- Model building and structural refinement --- p.18 / Chapter 2.4.3 --- Crystallization of Hu CT AcP -substate analogue complex --- p.19 / Chapter 2.5 --- Enzymatic Assay --- p.21 / Chapter 2.5.1 --- Preparation of benzoyl phosphate --- p.21 / Chapter 2.5.2 --- Purity check of the BP synthesized --- p.22 / Chapter 2.5.3 --- Determination of kinetic parameters of Hu CT AcP --- p.25 / Chapter 2.5.4 --- Determination of Ki value of substrate analogue --- p.27 / Chapter 2.6 --- Isothermal titration calorimetry --- p.28 / Chapter 2.7 --- Reagents and Buffers --- p.30 / Chapter 2.7.1 --- Reagent for competent cell preparation --- p.30 / Chapter 2.7.2 --- Media for bacterial culture --- p.31 / Chapter 2.7.3 --- Reagent for SDS-PAGE --- p.32 / Chapter 2.7.4 --- Buffer for AcP purification --- p.33 / Chapter 2.7.5 --- Buffer for enzymatic assay and ITC --- p.33 / Chapter Chapter 3 --- Structural determination of human common-type acylphosphatase --- p.34 / Chapter 3.1 --- Introduction --- p.34 / Chapter 3.2 --- Expression and purification of Hu CT AcP --- p.35 / Chapter 3.3 --- Structure of Hu CT AcP was determined by X-ray crystallography --- p.37 / Chapter 3.3.1 --- Crystallization of Hu CT AcP --- p.37 / Chapter 3.3.2 --- Model building and structural refinement --- p.41 / Chapter 3.3.3 --- Hu CT AcP shares a same α/β sandwich fold structure as other AcP --- p.43 / Chapter 3.4 --- Discussion --- p.46 / Chapter 3.4.1 --- Active site structure of Hu CT AcP is the same as those of bovine CT AcP and Ph AcP --- p.46 / Chapter 3.4.2 --- Absence of salt bridge between the active site residue and the C-terminal may contribute to the higher catalytic efficiency of Hu CT AcP --- p.52 / Chapter Chapter 4 --- Characterization of interaction between acylphosphatase and substrate analogues --- p.56 / Chapter 4.1 --- Introduction --- p.56 / Chapter 4.2 --- Selected substrate analogues --- p.57 / Chapter 4.3 --- Characterization of AcP-substrate analogue interaction by enzymatic assay --- p.59 / Chapter 4.3.1 --- Enzyme kinetics of Hu CT AcP was determined by the continuous optical assay of BP hydrolysis --- p.59 / Chapter 4.3.2 --- Substrate analogues were found to be competitive inhibitor to the AcP-catalyzed BP hydrolysis --- p.61 / Chapter 4.3.3 --- S-BA was the best competitive inhibitor against AcP-catalyzed BP hydrolysis --- p.64 / Chapter 4.3.4 --- S-BA was shown to be a competitive inhibitor for both Hu CT and Ph AcP --- p.66 / Chapter 4.4 --- Characterization of AcP-substrate analogue interaction by thermodynamic study --- p.68 / Chapter 4.4.1 --- Enthalpy change was observed for the association between substrate analogue and AcP --- p.68 / Chapter 4.4.2 --- S-BA was shown to bind Hu CT AcP with high affinity in ITC study --- p.68 / Chapter 4.5 --- S-BA was found to be the best substrate analogue for AcP --- p.72 / Chapter 4.6 --- Discussion --- p.73 / Chapter 4.6.1 --- Structure-affinity study of substrate analogue reveals chemical structures essential to interaction with AcP --- p.73 / Chapter 4.6.2 --- Structure-affinity study of substrate analogues is consistent with docking model of AcP with acetyl phosphate --- p.75 / Chapter 4.6.3 --- Validation of docking model by crystal complex structure --- p.78 / Chapter 4.6.4 --- Structural basis of substrate inhibition in Hu CT AcP --- p.80 / Chapter 4.6.4.1 --- Substrate inhibition is observed in Hu CT AcP --- p.80 / Chapter 4.6.4.2 --- Non-productive binding and substrate inhibition in AcP --- p.80 / Chapter Chapter 5 --- Investigation on the effect of salt bridge on acylphosphatase- substrate analogue interaction --- p.84 / Chapter 5.1 --- Introduction --- p.84 / Chapter 5.2 --- Thermodynamic study on the binding of S-BA with AcPs --- p.87 / Chapter 5.2.1 --- Determination of thermodynamic parameters of interaction between AcP and substrate analogue --- p.87 / Chapter 5.2.2 --- Determination of thermodynamic parameters as a function of temperature --- p.90 / Chapter 5.3 --- Discussion --- p.93 / Chapter 5.3.1 --- The presence of salt bridge leads to a reduced flexibility at the substrate binding active site --- p.93 / Chapter 5.3.2 --- The single salt bridge reduces the flexibility of active site in both study on thermodynamics of binding and thermodynamics of activation --- p.94 / Chapter 5.3.3 --- Temperature dependence of the thermodynamic parameters and heat capacity change ΔCp --- p.97 / Chapter 5.3.3.1 --- Change in heat capacity reveals the nature of the complex interface --- p.97 / Chapter 5.3.3.2 --- Determination of heat capacity change ΔCp --- p.98 / Chapter Chapter 6 --- Structural determination of acylphosphatase-substrate analogue complex --- p.102 / Chapter 6.1 --- Introduction --- p.102 / Chapter 6.2 --- Soaking and cocrystallization failed to give cocrystal structure of Hu CT AcP and S-BA --- p.103 / Chapter 6.4 --- Discussion --- p.106 / Chapter 6.4.1 --- Hu CT AcP and S-BA is not compatible with cocrystal formation --- p.106 / Chapter 6.5 --- Future prospect --- p.107 / Chapter 6.5.1 --- Structure determination by NMR spectroscopy --- p.107 / Chapter 6.5.2 --- Structure determination of AcP with aluminofluoride complexes --- p.108 / Chapter Chapter 7 --- Conclusion --- p.109 / Reference --- p.112

Thesis (M.S.)--Rochester Institute of Technology, 1991. / Typescript. Includes bibliographical references (leaves 124-126).

Thèse--Sc. phys.--Lyon I, 1982. / 1982 d'après la déclaration de dépôt légal. Notes bibliogr.

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

Techn. Hochsch., Diss., 2005--Aachen.

Doctor of Philosophy / Department of Grain Science and Industry / Yong Cheng Shi / The reaction of starch and octenylsuccinic anhydride (OSA) produces lipophilic starch that has the ability to stabilize oil-in-water emulsions. The functional properties of octenylsuccinate (OS) starch depend on its molecular structure and distribution of OS groups. Structures of OSA and OS starches were investigated by NMR spectroscopy. In granular OS starches, OS groups were substituted at O-2, O-3 positions, but not the O-6 position. Distribution of OS groups was investigated by enzyme hydrolysis followed by chromatography analysis. OS substitution predominantly occurred at the amorphous region of the starch granules. OS starch of degree of substitution (DS) 0.018 had OS groups located close to the branching points, whereas the OS substitution in OS starch of DS 0.092 occurred near non-reducing ends as well as the branching points. OS starches with different substitution patterns were prepared from two approaches. OS starches from the first approach had OS substitution near the branching points or non-reducing ends, whereas OS starches from the second approach had OS groups distributed randomly throughout the starch chains. A method of preparing OS starch by dry heating a mixture of waxy maize starch and OSA was developed. The optimum reaction was investigated and found to be pH 8.5 by addition of 3% NH4HCO3, 180 °C and 2 h. Reaction efficiency of ca. 90% was obtained at OSA levels from 1 to 6%. The OS starch had a DS of 0.0202 with 98% solubility when reacted with 3% OSA. Transglucosidation occurred during the reaction. The OS starch had a degree of branching of 19.8 %. The highly debranched OS starch showed excellent emulsification property for vitamin E and vitamin A. The structural changes of insoluble native waxy maize starch granules to cold watersoluble pyrodextrin during dextrinization under acidic conditions were investigated. We proposed that the starch was hydrolyzed by acid in the amorphous regions. Unwinding of the double helices also occurred, and crystallite size decreased. Starch molecules were hydrolyzed into small molecule fractions but remain in a radial arrangement. Glycosyl linkages including - (1 2), -(1 6), -(1 2), and -(1 6) linkages were formed and the majority starch chain terminals were 1,6-anhydro- -D-glucopyranose. Transglucosidation occurred during dextrinization and the resulted pyrodextrin was highly branched.

Two sets of structures were determined by X-ray crystallographic techniques, one of maleic anhydride (2,5-furandione) and the other of 4-phenyl-4-p-bromophenylcyclohex-2-en-1-one and its photoproduct, trans-5-phenyl-6-p-bromophenylbicyclo[3.1.0]hexan-2-one. Analysis of maleic anhydride included a room temperature redetermination of the crystal structure. This was done to improve parameters and simplify comparison of the room temperature and low temperature data. The structure determination at 104k resulted in the location of bonding electrons in the double bond. Thermal motions of both sets of data showed that translational motion was greatest along an axis parallel to the carbonyl bonds. Libration was found to be greatest about this axis also. The second set of structures was done to examine the migration pattern of aryl groups upon irradiation of a diarylcyclohexenone. The major photoproduct was formed by migration of the p-bromophenyl group. The resulting bicyclohexanone had the aryl groups trans to each other. / Science, Faculty of / Chemistry, Department of / Graduate

No description available.

Thesis (Ph. D.)--University of Pennsylvania, 1926.