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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Book ChapterDOI
Sporophytic and Gametophytic Self-Incompatibility
H. Kaufmann,Hans-Hubert Kirch,Thomas Wemmer,A. Peil,Friedrich Lottspeich,Helmut Uhrig,Francesco Salamini,Richard D. Thompson +7 more
TL;DR: The main features of the best-studied self- incompatibility (SI) systems will be summarized, followed by a more detailed description of potato pistil proteins and their possible role in SI.
Journal ArticleDOI
Production of recombinant human beta2-microglobulin for scintigraphic diagnosis of amyloidosis in uremia and hemodialysis.
Reinhold P. Linke,Jürgen Schäeffer,Peter Gielow,Peter Lindner,Friedrich Lottspeich,Andreas Plückthun,Elisabeth H. Weiss +6 more
TL;DR: This rhbeta2mH5 preparation is suitable for detecting amyloid-containing organs of the beta2m-class in vivo and fulfils the requirements of a tracer for common use.
Journal ArticleDOI
Nucleotide sequence of a putative succinate dehydrogenase operon in Thermoplasma acidophilum
TL;DR: Protein sequence comparison revealed significant homologies to the fumarate reductase and succinate dehydrogenase of other bacteria and three genes in the typical arrangement of an operon were revealed.
Journal ArticleDOI
Determination of the stoichiometry of protein complexes using liquid chromatography with fluorescence and mass spectrometric detection of fluorescently labeled proteolytic peptides
TL;DR: A method for the determination of the stoichiometry of protein complexes has been developed, which is based on proteolytic digestion of the complex, labeling with a fluorescent reagent, specific for amino or sulfhydryl groups, and separation by liquid chromatography with fluorescence and mass spectrometric detection.
Journal ArticleDOI
Purification and partial amino acid sequences of the enzyme vinorine synthase involved in a crucial step of ajmaline biosynthesis
Irina Gerasimenko,Xueyan Ma,Y. V. Sheludko,Reinhard Mentele,Friedrich Lottspeich,Joachim Stöckigt +5 more
TL;DR: The acetyl-CoA-dependent enzyme vinorine synthase is probably a novel member of the BAHD enzyme super family and involved in natural plant product biosynthesis.