@article{MichelWachterSebald1979,
  author    = {Michel, R. and Wachter, E. and Sebald, Walter},
  title     = {Synthesis of a larger precursor for the proteolipid subunit of the mitochondrial ATPase complex of Neurospora crassa in a cell-free wheat germ system},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62789},
  year      = {1979},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{SebaldGrafLukins1979,
  author    = {Sebald, Walter and Graf, T. and Lukins, H. B.},
  title     = {The dicyclohexylcarbodiimide-binding protein of the mitochondrial ATPase complex from Neurospora crassa and Saccharomyces cerevisiae. Identification and isolation},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62792},
  year      = {1979},
  abstract  = {Incubation of mitochondria from Neuraspara crassa and Saccharomyces cerevisiae with the radioactive ATPase inhibitor [14C]dicyclohexylcarbodiimide results in the irreversible and rather specific labelling of a low-molecular-weight polypeptide. This dicyclohexylcarbodiimide-binding protein is identical with the smallest subunit (Mr 8000) of the mitochondrial ATPase complex, and it occurs as oligomer, probably as hexamer, in the enzyme protein. The dicyclohexylcarbodiimide-binding protein is extracted from whole mitochondria with neutral chloroformjmethanol both in the free and in the inhibitor-modified form. In Neuraspara and yeast, this extraction is highly selective and the protein is obtained in homogeneaus form when the mitochondria have been prewashed with certain organic solvents. The bound dicyclohexylcarbodiimide Iabel is enriched in the purified protein up to 50-fold compared to whole mitochondria. Based on the amino acid analysis, the dicyclohexylcarbodiimide-binding protein from Neurospora and yeast consists of at least 81 and 76 residues, respectively. The content of hydrophobic residues is extremely high. Histidine and tryptophan are absent. The N-terminal ~mino acid is tyrosine in Neuraspara and formylmethionine in yeast.},
  subject      = {Biochemie},
  language  = {en}
}
@article{TzagoloffMacinoSebald1979,
  author    = {Tzagoloff, A. and Macino, G. and Sebald, Walter},
  title     = {Mitochondrial genes and translation products},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-47408},
  year      = {1979},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{SebaldWernerWeiss1979,
  author    = {Sebald, Walter and Werner, S and Weiss, H},
  title     = {Biogenesis of mitochondrial membrane proteins in Neurospora crassa},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-82055},
  year      = {1979},
  abstract  = {no abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{SebaldWild1979,
  author    = {Sebald, Walter and Wild, G.},
  title     = {Mitochondrial ATPase complex from Neurospora crassa},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-82065},
  year      = {1979},
  abstract  = {The A TPase eomplex has been isolated from mitoehondria of N eurospora crassa by immunologieal teehniques. The protein ean be obtained rapidly and qua ntitatively in high purity by miero- or large-seale immunopreeipitation. Immunopreeipitation has been applied to labeled and doubly labeled mitoehondrial proteins in order to investigate the number and moleeular weights of subunit polypeptides , the site of synthesis of subunit polypeptides, and the dieycIohexyIcarbodiimide-binding protein . The A TPase complex obtained by large-seale immunopreeipitation has been used as starting ma terial for the isolation of hydrophobie polypeptides.},
  subject      = {Biochemie},
  language  = {en}
}
@article{SebaldNeupertWeiss1979,
  author    = {Sebald, Walter and Neupert, W. and Weiss, H.},
  title     = {Preparation of Neurospora crassa mitochondria},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-82070},
  year      = {1979},
  abstract  = {The fungus Neurospora crassa represents a eukaryotic cell with high biosynthetic activities. Cell mass doubles in 2-4 hr during expone ntial growth , even in simple salt media with sucrose as the sole carbon source. The microorgani sm forms a mycelium of long hyphae durlng vegetative growth . The mitochondria can be isolated under relatively gentle condi tions since a few breaks in the threadlike hyphae are sufficient to cause the outflow of the organelles. This article describes two methods for the physical disruption of the hyphae : (I) The cell s are opened in a grind mill between two rotating corundum di sks. This is a continuous and fast procedure and allows large- and small-scale preparations of mitochondria. (2) Hyphae are ground with sand in a mortar and pestle. This procedure can be applied to microscale preparations of mitochondria starting with minute amounts of cells. Other procedures for the isolation of Neurospora mitochondria after the physical di sruption or the enzymatic degradation of the cell wall have been described elsewhere},
  subject      = {Biochemie},
  language  = {en}
}
@article{GrafSebald1978,
  author    = {Graf, T. and Sebald, Walter},
  title     = {The dicyclohexylcarbodiimide-binding protein of the mitochondrial ATPase complex from beef heart. Isolation and amino acid composition},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62806},
  year      = {1978},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{WeissSebald1978,
  author    = {Weiss, H. and Sebald, Walter},
  title     = {Purification of cytochrome oxidase from Neurospora crassa and other sources},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-82082},
  year      = {1978},
  abstract  = {A chromatographic procedure 1 is described by means of which cytochrome oxidase has been purified from a variety of organisms including the fungus N eurospora crassa,2,3 the unicellular alga Po/ytoma mirum, 4 the insect Locusta migratoria ,5 the frog Xenopus muel/eri,4 and the mammal Rattus norwegicus. 4 This procedure can be used to equal effect for large-scale preparations, starting from grams of mitochondrial protein, or for small-scale preparations starting from milligrams. The cytochrome oxidase preparations from the different organisms are enzymically active. They show similar subunit compositions.},
  subject      = {Biochemie},
  language  = {en}
}
@article{Sebald1977,
  author    = {Sebald, Walter},
  title     = {Biogenesis of mitochondrial ATPase},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-47362},
  year      = {1977},
  abstract  = {No abstract available},
  subject      = {Biochemie},
  language  = {en}
}
@article{JacklSebald1975,
  author    = {Jackl, G. and Sebald, Walter},
  title     = {Identification of two products of mitochondrial protein synthesis associated with mitochondrial adenosine triphosphatase from Neurospora crassa},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-62812},
  year      = {1975},
  abstract  = {Soluble mitochondrial ATPase (F1) isolated from Neurospora crassa is resolved by dodecylsulfate- gel electrophoresis into five polypeptide bands with apparent molecular weights of 59000, 55000, 36000, 15000 and 12000. At least nine further polypeptides remain associated with ATPase after disintegration of mitochondria with Triton X-100 as shown by the analysis of an immunoprecipitate obtained with antiserum to F 1 A TPase. Two of the associated polypeptides with apparent molecular weights of 19000 and 11000 are translated on mitochondrial ribosomes, as demonstrated by incorporation in vivo of radioactive leueine in the presence of specific inhibitors of mitochondrial (chloramphenicol) and extramitochondrial ( cycloheximide) protein synthesis. The appearance of mitochondrial translation products in the immunoprecipitated A TPase complex is inhibited by' cycloheximide. The same applies for some of the extramitochondrial translation products in the presence of chloramphenicol. This suggests that both types of polypeptides are necessary for the assembly of the A TPase complex.},
  subject      = {Biochemie},
  language  = {en}
}