Spelling suggestions: "subject:"[een] NITROGEN"" "subject:"[enn] NITROGEN""
11 |
Studies on the regulation of nitrogenase in Rhodospirillum rubrum, and on the inhibition by H₂ of nitrogenase from Klebsiella pneumoniaeGuth, Joseph H. January 1983 (has links)
Thesis (Ph. D.)--University of Wisconsin--Madison, 1983. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 147-148).
|
12 |
The production of nitrogen gas under anoxic conditionsCrane, John Stephen. January 1963 (has links)
Thesis (M.S.)--University of Wisconsin--Madison, 1963. / Typescript. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves [43-48]).
|
13 |
Studies in urinary nitrogen excretionKies, Constance, January 1960 (has links)
Thesis (M.S.)--University of Wisconsin--Madison, 1960. / Typescript. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.
|
14 |
Property deviations of nitrogenPanton, Ronald L. January 1962 (has links)
Thesis (M.S.)--University of Wisconsin--Madison, 1962. / Typescript. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves [95]-96).
|
15 |
The utilization by human subjects of nitrogen from beef round and beef heartKunerth, Bernice Lydia January 1933 (has links)
Typescript, etc.
|
16 |
A spectroscopic investigation of the formation of active nitrogenTregidga, Angus C. January 1935 (has links)
[No abstract available] / Science, Faculty of / Physics and Astronomy, Department of / Graduate
|
17 |
Engineering homoaromatic substrate specificity into aliphatic-specific Geobacillus pallidus RAPc8 nitrile hydrataseParikshant Kowlessur January 2007 (has links)
<p>Geobacillus pallidus RAPc8 is a thermophilic nitrile-degrading isolate, obtained from thermal sediment samples of a New Zealand hot spring. The G. pallidus RAPc8 NHase gene has been cloned and expressed in E. coli. The recombinant NHase exhibits nitrile-degrading activity at 50 ° / C, capable of degrading branched, linear and cyclic heteroaromatic nitrile substrates. However, no activity was found on homoaromatic nitrile substrates such as benzonitrile. In the present study, high levels of activity on benzonitrile were detected with a double mutant &beta / F52G&beta / F55L. Kinetic analysis on the mutant enzyme showed an 8-fold decrease in KM with benzonitrile (0.3mM) compared to acrylonitrile (2.6mM). Specificity constants (kcat/KM) of 5900 and 450 s-1.mM-1 were obtained for the double mutant on benzonitrile and acrylonitrile respectively. The amino acid residues lining the substrate channel were identified and the geometric dimensions measured. Cavity calculations revealed a 29% increase in volume and a 13% increase in inner surface area for the substrate channel of the double mutant when compared to the wild type. Surface representation of the wild type structure revealed two extended, curved channels, which are accessible to the bulk solvent from two locations in the heterodimer. The removal of the &beta / F52 may have contributed to the presence of a single channel with two opposing openings across the dimers with no internal blockage. Normal Mode Analysis calculations also indicate a higher intrinsic flexibility of the mutant relative tothe wild type enzyme. The increased flexibility within the mutant NHase could have introduced a functionally relevant aromatic substrate recognition conformation</p>
|
18 |
Screening for subtate tolerant Geobacillus pallidus RAPc8 nitrile hydrataseMketsu, Moses Clive Masisange January 2009 (has links)
<p>In this study G. pallidus RAPc8 NHase mutants were screened for reduced substrate inhibition compared to the wild type enzyme. Wild type and mutant enzymes were expressed and purified using hydrophobic interaction chromatography. Amidase coupled enzyme stop assays were conducted using 3-cyanopyridine as a substrate, whereas continuous enzyme kinetics were conducted using acrylonitrile as a substrate.</p>
|
19 |
Screening for subtate tolerant Geobacillus pallidus RAPc8 nitrile hydrataseMketsu, Moses Clive Masisange January 2009 (has links)
<p>In this study G. pallidus RAPc8 NHase mutants were screened for reduced substrate inhibition compared to the wild type enzyme. Wild type and mutant enzymes were expressed and purified using hydrophobic interaction chromatography. Amidase coupled enzyme stop assays were conducted using 3-cyanopyridine as a substrate, whereas continuous enzyme kinetics were conducted using acrylonitrile as a substrate.</p>
|
20 |
Engineering homoaromatic substrate specificity into aliphatic-specific Geobacillus pallidus RAPc8 nitrile hydrataseParikshant Kowlessur January 2007 (has links)
<p>Geobacillus pallidus RAPc8 is a thermophilic nitrile-degrading isolate, obtained from thermal sediment samples of a New Zealand hot spring. The G. pallidus RAPc8 NHase gene has been cloned and expressed in E. coli. The recombinant NHase exhibits nitrile-degrading activity at 50 ° / C, capable of degrading branched, linear and cyclic heteroaromatic nitrile substrates. However, no activity was found on homoaromatic nitrile substrates such as benzonitrile. In the present study, high levels of activity on benzonitrile were detected with a double mutant &beta / F52G&beta / F55L. Kinetic analysis on the mutant enzyme showed an 8-fold decrease in KM with benzonitrile (0.3mM) compared to acrylonitrile (2.6mM). Specificity constants (kcat/KM) of 5900 and 450 s-1.mM-1 were obtained for the double mutant on benzonitrile and acrylonitrile respectively. The amino acid residues lining the substrate channel were identified and the geometric dimensions measured. Cavity calculations revealed a 29% increase in volume and a 13% increase in inner surface area for the substrate channel of the double mutant when compared to the wild type. Surface representation of the wild type structure revealed two extended, curved channels, which are accessible to the bulk solvent from two locations in the heterodimer. The removal of the &beta / F52 may have contributed to the presence of a single channel with two opposing openings across the dimers with no internal blockage. Normal Mode Analysis calculations also indicate a higher intrinsic flexibility of the mutant relative tothe wild type enzyme. The increased flexibility within the mutant NHase could have introduced a functionally relevant aromatic substrate recognition conformation</p>
|
Page generated in 0.0416 seconds