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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Purification and characterization of a membrane-bound acid phosphatase of Leishmania mexicana.
TL;DR: As defined by the reaction with monoclonal antibodies, Leishmania mexicana promastigotes contain two acid phosphatases which together comprise about 90% of the cellular activity.
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Equalizer technology--Equal rights for disparate beads.
TL;DR: The results show that ProteoMiner or the different Sepabeads behave surprisingly similarly in the separation of complex protein mixtures, where diversity in surface ligands plays only a negligible role.
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Protein stoichiometry of a multiprotein complex, the human spliceosomal U1 small nuclear ribonucleoprotein: absolute quantification using isotope-coded tags and mass spectrometry.
Elisabeth O. Hochleitner,Berthold Kastner,Thomas Fröhlich,Alexander Schmidt,Reinhard Lührmann,Georg J. Arnold,Friedrich Lottspeich +6 more
TL;DR: The human U1 snRNP (small nuclear ribonucleoprotein) was denatured, digested completely with an endoproteinase and labeled with an amine-specific tag as discussed by the authors.
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Identification of an anion-specific channel in the cell wall of the Gram-positive bacterium Corynebacterium glutamicum
Noelia Costa-Riu,Elke Maier,Andreas Burkovski,Reinhard Krämer,Friedrich Lottspeich,Roland Benz +5 more
TL;DR: The gene products PorBCglut and PorCCglut represent obviously other permeability pathways for the transport of hydrophilic compounds through the cell wall of C. glutamicum.
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Production and characterization of recombinant mouse neurotrophin‐3
TL;DR: Neurotrophin-3 (NT-3) is a neurotrophic-factor that has recently been cloned on the basis of its structural similarity to other members of the nerve growth factor (NGF) gene family.