@article{SebaldHofstoetterHackeretal.1969,
  author    = {Sebald, Walter and Hofst{\"o}tter, T. and Hacker, D. and B{\"u}cher, T.},
  title     = {Incorporation of amino acids into mitochondrial protein of the flight muscle of Locusta migratoria in vitro and in vivo in the presence of cycloheximide},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62919},
  year      = {1969},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{KoenigSchefferBremmetal.1985,
  author    = {K{\"o}nig, W and Scheffer, J. and Bremm, K. D. and Hacker, J{\"o}rg and Goebel, W.},
  title     = {The role of bacterial adherence and toxin production from E. coli on leukotriene generation from human polymorphonuclear granulocytes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40295},
  year      = {1985},
  abstract  = {No abstract available},
  language  = {en}
}
@inproceedings{MochHoschuetzkyHackeretal.1987,
  author    = {Moch, Thomas and Hosch{\"u}tzky, Heinz and Hacker, J{\"o}rg and Kr{\"o}nke, Klaus-D. and Jann, Klaus},
  title     = {Isolation and characterization of the \(\alpha\)-Sialyl-\(\beta\) 2-3-Galactosyl (S)-Specific Adhesin fimbriated Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40330},
  year      = {1987},
  abstract  = {The \(\alpha\)-Sialyl-\(\beta\) 2-3-Galactosyl-specific adhesin (S adhesin) was isolated from cells of a recombinant Escherichia coli K-12 strain expressing the S-flmbrial adhesin complex. A crude cell extract was partiaUy dissociated into fimbriae and an adhesin-enriched fraction by heating to 7O°C. From the latter, adhesin was purified to apparent homogeneity (by fast protein liquid chromatography, immunoblot, and NaDodSO\(_4\)/PAGE) by differential ammonium sulfate precipitation, dissociation in 8 M guanidine hydrochloride, and high-resolution anion-exchange chromatography in 8 M urea. The purified adhesin formed an aggregate of M\(_r\)\(\approx\)10\(^6\) that was made up of one type of 12-kDa polypeptide (fimbrillin is 16.5 kDa). It had pI value of 4.7 (fimbriae has a pI value of 6). Adhesin and fimbrillin had different amino add compositions. The purified adhesins agglutinated human and bovine erythrocytes with the same speclfkity as the whole bacteria; purified fimbriae were not adhesive. Monoclonal anti-adhesin and anti-fimbriae antibodies were obtained. Monoclonal antiadhesin, but none of the anti-fimbriae, antibodies inhibited the agglutination of erythrocytes. The anti-adhesive antibodies were used in immuno-gold electron microscopy to localize adhesin exclusively on the fimbriae, with a possible preference to their tips.},
  language  = {en}
}