The search result changed since you submitted your search request. Documents might be displayed in a different sort order.
  • search hit 71 of 75
Back to Result List

N,N'-dicyclohexylcarbodiimide binds specifically to a single glutamyl residue of the proteolipid subunit of the mitochondrial adenosinetriphosphatases from Neurospora crassa and Saccharomyces cerevisiae

Please always quote using this URN: urn:nbn:de:bvb:20-opus-47394
  • T~e N,N'-dicrclohexylcarbodiimide-binding proteolipid subumt of the mitochondrial adenosinetriphosphatases (ATP phosphohydrolase, EC 3.6.1.3) of Neurosporacrassa and Saccharomyces cerevisiae were purified from mitochondria incubated with the radioactively labeled inhibitor. The specifically labeled subunit was cleaved with cyanogen bromide and N-bromosuccinimide, and the resultant fragments were separated by gel chromatography in the presence of 80% (vol/vol) formic acid. The N,N'-dicyclohexylcarbodiimide label was recovered in each organismT~e N,N'-dicrclohexylcarbodiimide-binding proteolipid subumt of the mitochondrial adenosinetriphosphatases (ATP phosphohydrolase, EC 3.6.1.3) of Neurosporacrassa and Saccharomyces cerevisiae were purified from mitochondria incubated with the radioactively labeled inhibitor. The specifically labeled subunit was cleaved with cyanogen bromide and N-bromosuccinimide, and the resultant fragments were separated by gel chromatography in the presence of 80% (vol/vol) formic acid. The N,N'-dicyclohexylcarbodiimide label was recovered in each organism exclusively in a 17-residue fragment. Further analysis by automated solid-phase Edman degrada.ti.on revealed tha~ the bound label was present at only one positIOn, correspondmg to a glutamyl residue. The NN'~ icyc~ohexyl~a~bodiiJ?1~de-'!l0dified glutamyl residue is the ~nly Id~ntIcal aCidic posItIon m both proteins and occurs in the middle of a hydrophobic sequence of about 25 residues.show moreshow less

Download full text files

Export metadata

Additional Services

Share in Twitter Search Google Scholar Statistics
Metadaten
Author: Walter Sebald, Werner Machleidt, Elmar Wachter
URN:urn:nbn:de:bvb:20-opus-47394
Document Type:Journal article
Faculties:Medizinische Fakultät / Theodor-Boveri-Institut für Biowissenschaften
Language:English
Year of Completion:1980
Source:In: Proceedings of the National Academy of Sciences of the United States of America (1980) 77, 2, 785-789.
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften
GND Keyword:Dicyclohexylcarbodiimid; Aminosäuren
Tag:amino acid sequence; automated solid-phase Edman degradation; inhibition of H+ translocation
Release Date:2010/12/17
Licence (German):License LogoDeutsches Urheberrecht