F
Friedrich Lottspeich
Researcher at Max Planck Society
Publications - 449
Citations - 31053
Friedrich Lottspeich is an academic researcher from Max Planck Society. The author has contributed to research in topics: Peptide sequence & Amino acid. The author has an hindex of 94, co-authored 449 publications receiving 30250 citations. Previous affiliations of Friedrich Lottspeich include Technische Universität Darmstadt & University of Marburg.
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Journal ArticleDOI
Purification of the synaptic vesicle-binding protein physophilin. Identification as 39-kDa subunit of the vacuolar H(+)-ATPase.
TL;DR: Results argue against a docking role of physophilin/Ac39 in synaptic vesicle exocytosis, with lesser amounts being present in synaptic plasma membrane fractions.
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Identification of stress proteins in endothelial cells
TL;DR: The major stress proteins in human endothelial cells were separated by two‐dimensional polyacrylamide gel electrophoresis with immobilized pH gradients in the first dimension and identified by immunoblotting and either N‐terminal or internal amino acid sequencing, respectively.
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Preparative high-yield electroelution of proteins after separation by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and its application to analysis of amino acid sequences and to raise antibodies.
Toshitaka Ohhashi,Chie Moritani,Hiromi Andoh,Sachiko Satoh,Shinji Ohmori,Friedrich Lottspeich,Mikiko Ikeda +6 more
TL;DR: A method for the preparative high-yield electroelution of proteins from SDS-polyacrylamide gel strips, applicable to the purification of proteins required for N-terminal amino acid sequencing and to raise antibodies was established.
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The Type IV Secretion System Component VirB5 Binds to the trans-Zeatin Biosynthetic Enzyme Tzs and Enables Its Translocation to the Cell Surface of Agrobacterium tumefaciens
TL;DR: The fact that Tzs localizes on the cell surface suggests that it may contribute to the interaction of Agrobacterium with plants, and the VirB5-Tzs interaction was confirmed using pulldown assays with purified proteins and the yeast two-hybrid system.