TY  - JOUR
A1  - Sebald, Walter
A1  - Weiss, H.
A1  - Jackl, G.
T1  - Über die Abhängigkeit des Zusammenbaus der Cytochromoxidase von der Anwesenheit der Produkte der mitochondrialen Proteinsynthese
T1  - Dependence of the structure of cytochrome oxidase on the presence of products from mitochondrial protein synthesis
N2  - no abstract available
KW  - Physiologische Chemie
Y1  - 1972
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-84192
ER  - 
TY  - JOUR
A1  - Jackl, G.
A1  - Sebald, Walter
T1  - Identification of two products of mitochondrial protein synthesis associated with oligomycin-sensitive ATPase from Neurospora crassa
N2  - no abstract available
KW  - Physiologische Chemie
Y1  - 1974
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-82093
ER  - 
TY  - JOUR
A1  - Sebald, Walter
A1  - Weiss, H.
A1  - Jackl, G.
T1  - Inhibition of the assembly of cytochrome oxidase in Neurospora crassa by chloramphenicol
N2  - Cytochrome oxidasewas prepared from Neurospora crassa by chromatography on oleyl polymethacrylic acid resin and separated into seven polypeptides by polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate. Incorporation oflabelled amino acids into the single polypeptideswas investigated after a pulse labelling in the absence and presence of chloramphenicol, and afterwashing out the inhibitor. Chloramphenicol (4 mg/ml) inhibited amino acid incorporation into all polypeptides 90-95%• while labeHing of the whole membrane protein was inhibited only 30%• Mter washing out the inhibitor and further growth of the cells. the four smaller polypeptides were highly labelled, whereas the other polypeptides showed only a. small increase in radioactivity. It is concluded that the four small-sized polypeptides of cytochrome oxidase are synthesized but not integrated into the functional enzyme under the action of chloramphenicol.
KW  - Biochemie
Y1  - 1972
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-62852
ER  - 
TY  - JOUR
A1  - Jackl, G.
A1  - Sebald, Walter
T1  - Identification of two products of mitochondrial protein synthesis associated with mitochondrial adenosine triphosphatase from Neurospora crassa
N2  - 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.
KW  - Biochemie
Y1  - 1975
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-62812
ER  -