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Metapyrocatechase: catechol oxidation in Azotobacter vinelandiiSangster, Paul Edward, 1939- January 1968 (has links)
No description available.
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The modulation of the ATPase activity of spinach chloroplast coupling factor 1 by ADP and phosphateDunham, Kristine René. January 1981 (has links)
Thesis (Ph. D.)--University of Wisconsin--Madison, 1981. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 145-154).
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Suiwering en aspekte van die katalitiese meganisme van 'n esterase van Cucurbita MaximaGrobler, Amanda 11 November 2015 (has links)
M.Sc. (Biochemistry) / Please refer to full text to view abstract
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Enzymatic studies of conidial attachment and lectin-gold histochemicalinvestigation of the extracellular mucilages of Lemonniera aquatica deWild. and Mycocentrospora filiformis (Petersen) Iqbal歐慧婷, Au, Wai-ting, Doris. January 1993 (has links)
published_or_final_version / Botany / Doctoral / Doctor of Philosophy
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Kinetic studies on the emulsion liquid membrane extraction of lactic acidChaudhuri, Julian Brajendra January 1990 (has links)
No description available.
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Isolation of phenylalanine hydroxylases and enzymatic studies with 3- and 4- pyridylalanineHan, Jin Hee 05 1900 (has links)
No description available.
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A kinetic and resonance Raman spectroscopic investigation of protocatechuate-3,4-dioxygenasePhillips, Robert Stephen 08 1900 (has links)
No description available.
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Noncovalent modification of L-glutamic acid dehydrogenase from bovine liver /Kempner, David Howard. January 1975 (has links)
Thesis (Ph.D.)--Tufts University, 1975. / Submitted to the Dept. of Chemistry. Access restricted to members of the Tufts University community. Also available via the World Wide Web;
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Enzymatic studies of conidial attachment and lectin-gold histochemical investigation of the extracellular mucilages of Lemonniera aquatica de Wild. and Mycocentrospora filiformis (Petersen) Iqbal /Au, Wai-ting, Doris. January 1993 (has links)
Thesis (Ph. D.)--University of Hong Kong, 1993.
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The conformational stability of a detoxification enzyme widely used as a fusion-protein affinity tag.Kaplan, Warren H January 1997 (has links)
A thesis submitted to the Faculty of Science, University of the Witwatersrand, in
fulfilment of the requirements for the degree of Doctor of Philosophy. / A glutathione S-transferase (Sj26GST) from Schistosoma japonicum, which functions in
the parasite's Phase II detoxification pathway, is expressed by the Pharmacia pGEX-2T
plasmid and is widely used as a fusion-protein affinity tag. It contains all 217 residues
of Sj26GST and an ad titional 9-residue peptide linker with a thrombin cleavage site at
its C-terminus. Size-exclusion HPLC (SEC-HPLC) and SDS-PAGE studies indicate that
purification of the homodimeric protein under nonreducing conditions results in the
reversible for-ration of significant amounts of 160 -kDa and larger aggregates without
a loss in catalytic activity. The basis for oxidative aggregation can be ascribed to the high
degree of exposure of the four cysteine residues per subunit. The conformational stability
of the dimeric protein was studied by urea- and temperature-induced unfolding
techniques. Fluorescence-spectroscopy, SEC-HPLC, urea- and temperature-gradient gel
electrophoresis, ultraviolet melting, differential scanning micro calorimetry , and enzyme
activity were employed to monitor structural and functional changes. The unfolding data
indicate the absence of thermodynamically stable intermediates and that the
umolding/refolding transition is a two-state process involving folded native dimer and
unfolded monomer. The stability of the protein was found to be dependent on its
concentration with a ~GO(H20) = 26 ±1.7 kcal/mol. The conformational stability was
unchanged in the presence of the leading antischistosomal drug Praziquantel, which
bound the protein with a Kd = 9 ±1.8 p,M. The strong relationship observed between
the m-v,llue and the size of the protein indicates that the amount of protem. surface
exposed to solvent upon unfolding is the major structural de.erminant for the dependence
of the protein's free energy of unfolding on urea concentration. 'Ihermograms obtained
by differential scanning calorimetry also fitted to a two-state irreversible unfolding
transition, both in the presence and absence of Praziquantel, with values of ~Cp = 1779
cal mol-IK-I
, ~HcaI = 227 kcal/mol, AHVH ::::::233 kcal/mol (r :::::~:HVHIAlIcal = 1.02)
and AS = 354 cal mol''K". The low ~Cp and ~S, when compared with the theoretically
determined values, implied that the thermal denaturation of Sj26GST did not result in
complete unfolding of the protein, / Andrew Chakane 2018
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