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The Global ETD Search service is a free service for researchers
to find electronic theses and dissertations. This service is
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Networked Digital Library of Theses and Dissertations.
Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.
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Showing 91 to 100 of 2711 (0.083 seconds)Spelling suggestions: "subject:"purification."" "subject:"urification.""
| 91 |
Hydrodynamic behaviour of biological aggregates: settling and coagulation with small particlesYuan, Yuan, 袁媛 January 2000 (has links)
published_or_final_version / Civil Engineering / Master / Master of Philosophy
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| 92 |
Some characteristics of the calcium-activated protease from bovine cardiac muscleTan, Fuji January 1981 (has links)
No description available.
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| 93 |
PURIFICATION AND CHARACTERIZATION OF BOVINE LIVER ORNITHINE DECARBOXYLASEHaddox, Mari Kristine January 1980 (has links)
Ornithine decarboxylase has been purified to apparent homogeneity from thioacetamide-stimulated calf liver. The purification process, which has been developed to circumvent the lability of the enzyme, employs ion exchange chromatography, gel filtration, hydroxylapatite chromatography, non-denaturing gel electrophoresis, and sulfhydryl affinity chromatography. The enzyme is purified 71,500-fold to a final specific activity of 286,000 pmol/min/mg protein. Non-denaturing gel electrophoresis indicates a single protein present in the final preparation. The enzyme has a Stokes radius of 3.14 nm as indicated by gel filtration and a monomeric molecular weight of 52,000 daltons as indicated by denaturing gel electrophoresis. The K(m) values for ornithine and pyridoxal phosphate are 0.16 mM and 2.5 μM, respectively. Putrescine inhibits the enzyme (Kᵢ 10mM). The existence of three ionic forms of ornithine decarboxylase is suggested by fractionation of the preparation by gradient sievorptive chromatography. Mammalian ornithine decarboxylase is apparently a metalloenzyme. A variety of structurally distinct metal chelators inhibit the enzyme. A non-chelating analog of the most potent chelator, 1,10-phenanthroline, is without effect. The order of efficacy of the chelators suggests the involvement of a metal from the transition series. Incubation of the enzyme with charcoal or Cibacron Blue-Agarose results in a loss of catalytic activity suggesting that the ornithine decarboxylase may also contain a bound nucleotide.
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| 94 |
Soil filtration of activated sludge effluentAdams, William Pearson, 1945- January 1971 (has links)
No description available.
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| 95 |
Water purification by forced-flow electrophoresisCooper, Frederick Christian, 1940- January 1964 (has links)
No description available.
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| 96 |
Biological removal of phosphates from aquatic mediaGreer, Douglas Edwin, 1941- January 1971 (has links)
No description available.
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| 97 |
Effect of molecular weight on polymer filter aidsBurr, John Gregory, 1946- January 1972 (has links)
No description available.
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| 98 |
Effect of mixing and surfactants on oxygenation capacity by surface entrainment aerationChen, Juinn-Ie, 1938- January 1967 (has links)
No description available.
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| 99 |
Nucleation kinetics of the potassium chloride-water system with predictions of crystal-size distributions in crystallizers of complex configurationMetchis, Steven Geoffrey, 1951- January 1974 (has links)
No description available.
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| 100 |
Optimization of the polymeric coagulation processMansfield, Clifford Shedd, 1948- January 1972 (has links)
No description available.
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