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  • About
  • The Global ETD Search service is a free service for researchers to find electronic theses and dissertations. This service is provided by the 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.
1

Binding partners for mouse acetylcholinesterase in the central nervous system

Paraoanu, Laura Elena. January 2004 (has links) (PDF)
Darmstadt, Techn. Univ., Diss., 2004.
2

The development of a method for the utilization of progress curves to determine kinetic parameters and its application to horse serum cholinesterase

Balcom, Jean Kent, January 1969 (has links)
Thesis (Ph. D.)--University of Wisconsin--Madison, 1969. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.
3

Intramolecular facilitation of dealkylation of a phosphonate ester, a model of ageing in the reactivation of inhibited cholinesterase

Mlodozeniec, Arthur R. January 1964 (has links)
Thesis (Ph. D.)--University of Wisconsin--Madison, 1964. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 52-56).
4

Post-translational modifications of acetylcholinesterase

Giles, Kurt January 1994 (has links)
No description available.
5

Studies on human red cell cholinesterase in relation to muscle disease.

Robinson, Joseph Desmond, January 1900 (has links)
Thesis (M. Phil.)--University of Hong Kong, 1978. / Xeorx copy of typescript.
6

Micro-analysis of neostigmine bromide from plasma in surgical concentrations by Richard Jennings Helms

Helms, Richard Jennings, 1945- January 1976 (has links)
No description available.
7

Studies concerning chemical warfare agents Part A. The thermodynamic activity of sarin in solution. Part B. Exploratory investigation of the effects of solvents on skin lipids and skin penetration /

Kinkel, Arlyn W. January 1958 (has links)
Thesis (Ph. D.)--University of Wisconsin--Madison, 1958. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 81-84).
8

Studies on human red cell cholinesterase in relation to muscle disease

Robinson, Joseph Desmond, January 1900 (has links)
Thesis (M.Phil.)--University of Hong Kong, 1978. / Also available in print.
9

Untersuchungen zur Aktivität der Plasma-Cholinesterase bei gesunden und erkrankten Zwergkaninchen

Ludwig, Anja. Unknown Date (has links) (PDF)
Tierärztl. Hochsch., Diss., 2004--Hannover.
10

Amino Acids Defining the Acyl Pocket of an Invertebrate Cholinesterase

Pezzementi, Leo, Johnson, Kimberly, Tsigelny, Igor, Cotney, Justin, Manning, Elizabeth, Barker, Andrew, Merritt, Sarah 01 January 2003 (has links)
Amphioxus (Branchiostoma floridae) cholinesterase 2 (ChE2) hydrolyzes acetylthiocholine (AsCh) almost exclusively. We constructed a homology model of ChE2 on the basis of Torpedo californica acetylcholinesterase (AChE) and found that the acyl pocket of the enzyme resembles that of Drosophila melanogaster AChE, which is proposed to be comprised of Phe330 (Phe290 in T. californica AChE) and Phe440 (Val400), rather than Leu328 (Phe288) and Phe330 (Phe290), as in vertebrate AChE. In ChE2, the homologous amino acids are Phe312 (Phe290) and Phe422 (Val400). To determine if these amino acids define the acyl pocket of ChE2 and its substrate specificity, and to obtain information about the hydrophobic subsite, partially comprised of Tyr352 (Phe330) and Phe353 (Phe331), we performed site-directed mutagenesis and in vitro expression. The aliphatic substitution mutant F312I ChE2 hydrolyzes AsCh preferentially but also butyrylthiocholine (BsCh), and the change in substrate specificity is due primarily to an increase in kcat for BsCh; Km and K ss are also altered. F422L and F422V produce enzymes that hydrolyze BsCh and AsCh equally due to an increase in kcat for BsCh and a decrease in kcat for AsCh. Our data suggest that Phe312 and Phe422 define the acyl pocket. We also screened mutants for changes in sensitivity to various inhibitors. Y352A increases the sensitivity of ChE2 to the bulky inhibitor ethopropazine. Y352A decreases inhibition by BW284c51, consistent with its role as part of the choline-binding site. Aliphatic replacement mutations produce enzymes that are more sensitive to inhibition by iso-OMPA, presumably by increasing access to the active site serine. Y352A, F353A and F353V make ChE2 considerably more resistant to inhibition by eserine and neostigmine, suggesting that binding of these aromatic inhibitors is mediated by π-π or cation-π interactions at the hydrophobic site. Our results also provide information about the aromatic trapping of the active site histidine and the inactivation of ChE2 by sulfhydryl reagents.

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