Martin Tögel

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Previous studies on the role of microtubule-associated protein 1B (MAP1B) in adapting microtubules for nerve cell-specific functions have examined the activity of the entire MAP1B protein complex consisting of heavy and light chains and revealed moderate effects on microtubule stability. Here we have analyzed the effects of the MAP1B light chain in the(More)
Recently, the concept of microtubule-associated protein 1B as an intracellular 2460 amino acid protein was challenged by the suggestion that only the N-terminal 1022 codons are utilized and encode the core protein of the extracellular proteoglycan claustrin (Burg and Cole (1994) J. Neurobiol. 25, 1-22). We expressed this N-terminal MAP1B fragment in tissue(More)
Transgenic rabbits carrying gene constructs encoding human nerve growth factor beta (hNGF-beta) cDNA were generated. Expression of hNGF-beta mRNA was restricted to the mammary gland of lactating rabbits. Western Blot analysis revealed a polypeptide of 13.2 kDa in the milk of transgenic animals. hNGF-beta was purified from the milk by a two-step(More)
Two polyclonal antibodies were raised against the gamma 1-subunit of gamma-aminobutyric acidA (GABAA) receptors. One of these antibodies could be used for the immunopurification of GABAA receptors containing gamma 1-subunits. These receptors exhibited [3H]muscimol and [3H]flunitrazepam binding, and their benzodiazepine binding properties were dramatically(More)
The microtubule-associated proteins 1B and 1A are synthesized as polyprotein precursors which are rapidly cleaved to give rise to heavy and light chains constituting the respective microtubule-associated protein 1B or microtubule-associated protein 1A complex. To identify domains necessary for precursor processing, we expressed microtubule-associated(More)
Two polyclonal antibodies were raised against the gamma 3-subunit of gamma-aminobutyric acidA (GABAA) receptors. These antibodies were able to precipitate GABAA receptors from brain membrane extracts, and the precipitated receptors exhibited benzodiazepine binding properties that were dramatically different from those of receptors precipitated by anti-gamma(More)
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