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An investigation of the effects of the Drosophila circadian clock mutation double-time[superscript s] on double-time protein levels, nuclear localization of PER and temperature compensationBao, Shu. January 1999 (has links)
Thesis (M.S.)--West Virginia University, 1999. / Title from document title page. Document formatted into pages; contains vi, 62 p. : ill. (some col.). Includes abstract. Includes bibliographical references (p. 35-42).
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Protein and cell patterning for cell-based biosensor applications /Veiseh, Mandana. January 2004 (has links)
Thesis (Ph. D.)--University of Washington, 2004. / Vita. Includes bibliographical references (leaves 222-246).
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Immobilisation of biomolecules onto organised molecular assemblies /Albers, Willem M. January 1999 (has links) (PDF)
Thesis (Ph. D.)--Cranfield University, 1999. / Includes bibliographical references. Also available on the World Wide Web.
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New micropatterning techniques for the spatial addressable immobilization of proteinsFilipponi, Luisa. January 2006 (has links)
Thesis (PhD) - Swinburne University of Technology, Industrial Research Institute Swinburne - 2006. / A thesis submitted in fulfilment of the requirements for the degree of Doctor of Philosophy, Industrial Research Institute Swinburne, Swinburne University of Technology - 2006. Typescript. Includes bibliographical references (p. 184-197).
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I. Isolation and characterization of covalent trypsin-soybean trypsin inhibitor adducts ; II. Immobilization of proteins by reductive alkylation with hydrophobic aldehydes ; III. Incorporation of insulin into a liposomal membrane /Wu, Hua-Lin January 1980 (has links)
No description available.
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Immobilization of proteins on porous polymer beads /Ampon, Kamaruzaman, January 1987 (has links)
No description available.
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Proteins colocalize in the boar cytoplasmic droplet /Fischer, Katherine A. January 2003 (has links)
Thesis (M.S.)--University of Missouri-Columbia, 2003. / Typescript. Includes bibliographical references (leaves 101-107). Also available on the Internet.
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Proteins colocalize in the boar cytoplasmic dropletFischer, Katherine A. January 2003 (has links)
Thesis (M.S.)--University of Missouri-Columbia, 2003. / Typescript. Includes bibliographical references (leaves 101-107). Also available on the Internet.
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FTIR-ATR characterization of hydrogel, polymer films, protein immobilization and benzotriazole adsorption on copper surfacePillai, Karthikeyan. Chyan, Oliver Ming-Ren, January 2007 (has links)
Thesis (M.S.)--University of North Texas, Dec., 2007. / Title from title page display. Includes bibliographical references.
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Antibody Microprobes for Detecting Neuropeptide ReleaseSteagall, Rebecca J., Williams, Carole A., Duggan, Arthur W. 24 October 2011 (has links)
Antibody-coated microprobes have been demonstrated to be useful for detecting the release of neuropeptide transmitters from discrete sites in the central nervous system (CNS). This technique uses glass micropipettes taken through a series of chemical coatings, starting with a γ- aminopropyltriethoxysilane solution and ending with the antibody specific to the peptide transmitter of interest. The key to the reliability and repeatability of the technique is a uniform, even coating of the siloxane polymer to the glass micropipette. The microprobes, as they are called following the completion of the coating process, are inserted stereotaxically into a specific area of the CNS and the physiological intervention is performed. Tip diameters are around 5-10 μm and, depending on the length of the pipette inserted into the CNS, diameters of the pipette shaft will approach 40-50 μm. Once removed, the microprobe is then incubated with the radiolabeled peptide. Binding of the radiolabeled peptide will occur to the antibody sites not occupied by the endogenously released peptide. The images of the microprobes on sensitive autoradiographic film are analyzed for differences in the optical density along a specified length of probe. Areas of lighter density signify sites along the microprobe where endogenous peptide was biologically released during the physiological intervention. Knowing the exact location of the probe tip in vivo in the CNS permits identification of neurophysiological sites corresponding along the length of the microprobe where the peptide was released.
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