Search Results - (Author, Cooperation:S. Stieger)
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1Latest Papers from Table of Contents or Articles in PressC. J. Anderson ; S. Bahnik ; M. Barnett-Cowan ; F. A. Bosco ; J. Chandler ; C. R. Chartier ; F. Cheung ; C. D. Christopherson ; A. Cordes ; E. J. Cremata ; N. Della Penna ; V. Estel ; A. Fedor ; S. A. Fitneva ; M. C. Frank ; J. A. Grange ; J. K. Hartshorne ; F. Hasselman ; F. Henninger ; M. van der Hulst ; K. J. Jonas ; C. K. Lai ; C. A. Levitan ; J. K. Miller ; K. S. Moore ; J. M. Meixner ; M. R. Munafo ; K. I. Neijenhuijs ; G. Nilsonne ; B. A. Nosek ; F. Plessow ; J. M. Prenoveau ; A. A. Ricker ; K. Schmidt ; J. R. Spies ; S. Stieger ; N. Strohminger ; G. B. Sullivan ; R. C. van Aert ; M. A. van Assen ; W. Vanpaemel ; M. Vianello ; M. Voracek ; K. Zuni
American Association for the Advancement of Science (AAAS)
Published 2016Staff ViewPublication Date: 2016-03-05Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsPublished by: -
2Articles: DFG German National LicensesStieger, S. ; Bütikofer, P. ; Wiesmann, U. N. ; Brodbeck, U.
Oxford, UK : Blackwell Publishing Ltd
Published 1989Staff ViewISSN: 1471-4159Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Abstract The mouse neuroblastoma cell line NB2A produces cellular and secreted acetylcholinesterase (AChE). After incubation of the cells for 4 days the ratio between AChE secreted into the medium and AChE in the cells was 1:1. The cell-associated enzyme could be subdivided into soluble AChE (25%) and detergent-soluble AChE (75%). Both extracts contained predominantly monomelic AChE (4.6S) and minor amounts of tetrameric AChE (10.6S), whereas the secreted AChE in the culture supernatant contained only the tetrameric form. All forms were partially purified by affinity chromatography. It could be demonstrated that the secretary and the intracellular soluble tetramers were hydrophilic, whereas the detergent-soluble tetramer was an amphiphilic protein. On the other hand the soluble and the detergent-soluble monomelic forms were amphiphilic and their activity depended on the presence of detergent. By digestion with proteinase K amphiphilic monomelic and tetrameric AChE could be converted to a hydrophilic form that no longer required detergent for catalytic activity. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of [3H]diisopropylfluorophosphate-labelled AChE gave one band at 64 kilodaltons (kD) under reducing conditions and two additional bands at 120 kD and 140 kD under nonreducing conditions.Type of Medium: Electronic ResourceURL: -
3Articles: DFG German National LicensesStaff View
ISSN: 1471-4159Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Proteolytic fragmentation of (3H]diisopropylflu-orophosphate-labelled catalytic subunits of different molecular forms of acetylcholinesterase demonstrates that all forms extracted from the electric organ from Torpedo marmorata are true acetylcholinesterases. This is supported by immunochemical results showing that the radiolabelled polypeptides are readily recognized by specific anti-acetyl-cholinesterase antibodies. Although distinct structural differences exist, all forms contain a similar peptide carrying the serine hydroxyl of the esteratic subsite. Dimeric, detergent-soluble acetylcholinesterase is present in the low-salt-soluble extract (Mr of the catalytic subunit 66,000) together with a monomeric form (apparent Mr 76,000). This monomeric polypeptide is hydrophilic, enzymatically inactive, and might represent a precursor of the asymmetric forms of acetylcholinesterase.Type of Medium: Electronic ResourceURL: -
4Articles: DFG German National LicensesStaff View
ISSN: 1471-4159Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: The membrane-bound acetylcholinesterase (AChE) from the electric organ of Torpedo marmorata was solubilized by Triton X-100 or by treatment with proteinase K and purified to apparent homogeneity by affinity chromatography. Although the two forms differed only slightly in their subunit molecular weight (66,000 and 65,000 daltons, respectively), considerable differences existed between native and digested detergent-soluble AChE. The native enzyme sedimented at 6.5 S in the presence of Triton X-100 and formed aggregates in the absence of detergent. The digested enzyme sedimented at 7.5 S in the absence and in the presence of detergent. In contrast to the detergent-solubilized AChE, the proteolytically derived form neither bound detergent nor required amphiphilic molecules for the expression of catalytic activity. This led to the conclusion that limited digestion of detergent-soluble AChE results in the removal of a small hydrophobic peptide which in vivo is responsible for anchoring the protein to the lipid bilayer.Type of Medium: Electronic ResourceURL: -
5Articles: DFG German National LicensesStaff View
ISSN: 0014-5793Keywords: Acetylcholinesterase ; Anchor peptide ; Hydrophobic labeling ; Membrane protein ; Proteolytic digestion ; Torpedo marmorataSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyPhysicsType of Medium: Electronic ResourceURL: -
6Articles: DFG German National LicensesStaff View
ISSN: 0300-9084Keywords: acetylcholinesterase ; enzymatic properties ; glycosyl-phosphatidylinositol anchor ; phosphatidylinositol-specific phospholipase CSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyType of Medium: Electronic ResourceURL: -
7Articles: DFG German National LicensesStaff View
ISSN: 0167-4838Keywords: Acetylcholinesterase ; Anti-CRD antibody ; Cross-reacting determinantSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyMedicineType of Medium: Electronic ResourceURL: -
8Articles: DFG German National LicensesStaff View
ISSN: 0304-4165Keywords: (Cytophaga sp.) ; Acetylcholinesterase ; Glycosylphosphatidylinositol ; Glycosylphosphatidylinositol-specific phospholipase C ; Phosphatidylinositol-specific phospholipase CSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyMedicinePhysicsType of Medium: Electronic ResourceURL: -
9Articles: DFG German National LicensesStaff View
ISSN: 1573-6830Keywords: acetylcholinesterase ; amino acid sequence ; amino acid analysis ; bovine brain ; bovine erythrocytesSource: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Summary 1. Comparison of partial amino acid sequences of G2-acetylcholinesterase (AChE) from bovine erythrocytes and G4-AChE from bovine caudate nucleus revealed no differences in primary structure between the two enyzmes. The first 33 residues of the N-terminal sequences were identical. 2. In addition, the amino acid sequences of four peptides generated by tryptic and cyanogen bromide cleavage were identical for bovine erthyrocyte and brain AChE, suggesting one identical major coding exon for the adult bovine AChE forms. Comparison of these sequences with that of fetal bovine serum AChE (Doctoret al., 1988), showed differences in residues 16, 181, 212, and 216. 3. Deglycosylation studies of the two adult enzyme forms revealed that the core protein of erythrocyte AChE has an approximately 4 kDa lower molecular mass than brain AChE. This most propably reflects differences in the C-terminal sequences of the two enzymes.Type of Medium: Electronic ResourceURL: