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Generating an expression construct and soluble protein for characterization studies of a putative RNA m5C methyltransferase, yeast ORF YNLO22cCraft, Jennifer Leigh January 2005 (has links)
RNA m5C methyltransferases are a group of enzymes that catalyze the transfer of a methyl group to a cytosine nucleotide of RNA. Only two of these enzymes have been well characterized: Fmu from E. coli and Trm4p from S. cerevisiae. YNLO22c is one of three ORFs identified in S. cerevisiae that have homology with both known and putative RNA m5C methyltransferases, but its encoded protein, YNLO22p, has not been confirmed to have enzyme activity. Verifying that YNLO22c encodes an RNA m5C methyltransferase will require adequate amounts of soluble YNLO22p for enzyme assays. A bacterial expression plasmid for YNLO22c was developed, but the result was insoluble protein. Therefore, several methods known to improve protein solubility were tested to develop a system in which a sufficient amount of soluble YNLO22p could be produced. Results of this study found that coexpression of YNLO22c with chaperone proteins can provide sufficient quantities of soluble YNLO22p. / Department of Biology
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Chemical extraction of recombinant protein from the cytoplasm of Escherichia coli / by Robert John Falconer.Falconer, Robert J. January 1997 (has links)
Two leaves of amendments in pocket on front end paper. / Bibliography: leaves 177-185. / xix, 194 leaves : ill. ; 30 cm. / Title page, contents and abstract only. The complete thesis in print form is available from the University Library. / Describes selective and nonselective procedures to extract recombinant protein from the cytoplasm of Escherichia coli. / Thesis (Ph.D.)--University of Adelaide, Dept. of Chemical Engineering, 1997
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Biochemical analysis of apoptosome formationKim, Hyun-Eui January 2006 (has links)
Dissertation (Ph.D.) -- University of Texas Southwestern Medical Center at Dallas, 2006. / Vita. Bibliography: p. 106-117
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Physicochemical properties of protein inclusion bodies /Wangsa-Wirawan, Norbertus Djajasantosa. January 1999 (has links) (PDF)
Thesis (Ph.D.)--University of Adelaide, Dept. of Chemical Engineering, 2000? / Bibliography: leaves 182-198.
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Expression of recombinant proteins in Escherichia coli under the transcriptional control of the cold-shock inducible cspA promoter /Vasina, Jess A., January 1997 (has links)
Thesis (Ph. D.)--University of Washington, 1997. / Vita. Includes bibliographical references (leaves [116]-124).
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Effect of recombinant porcine somatotropin (rpST) on placental and fetal growth in gilts /Sterle, Jodi A. January 1998 (has links)
Thesis (Ph. D.)--University of Missouri-Columbia, 1998. / Typescript. Vita. Includes bibliographical references (leaves 125-139). Also available on the Internet.
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Biochemical characterization of genetic recombination proteins /Houston, Peter Louis, January 1998 (has links)
Thesis (Ph. D.)--University of Texas at Austin, 1998. / Vita. Includes bibliographical references (leaves 147-163). Available also in a digital version from Dissertation Abstracts.
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Effect of recombinant porcine somatotropin (rpST) on placental and fetal growth in giltsSterle, Jodi A. January 1998 (has links)
Thesis (Ph. D.)--University of Missouri-Columbia, 1998. / Typescript. Vita. Includes bibliographical references (leaves 125-139). Also available on the Internet.
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Cloning expression and characterization of human oviductal C3 fragments /Kwok, Ka-leung. January 2005 (has links)
Thesis (M. Med. Sc.)--University of Hong Kong, 2005.
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An investigation of peptide-based translocating systems and their potential for gene therapyNwachuku, Julia Nonyelum Lucille January 2000 (has links)
No description available.
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