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- W2187105048 abstract "A AgtlObovine brain andaAgtllbovine heart cDNAlibrary werescreened with oligonucleotide probes corresponding topartial protein sequences directly determined fromtheisolated 51-kDa subunit ofthebovine respiratory- chain NADHdehydrogenase. Clones wereisolated that encode aprotein of464amino acids containing all the11partial tryptic peptide sequences determined fromthe51-kDa subunit. The size andaminoacid composition ofthis protein agree with those determined forthepurified 51-kDa subunit. Furthermore, this protein contains aputative NADH-binding domain, apossible FMN-binding site, andaputative binding site foraniron-sulfur duster. Theabove evidence indicates that thecloned protein is the51-kDa subunit oritsprecursor. A search forsequence similarity withproteins intheProtein Identification Resource data basehasrevealed that the51-kDa subunit has32%amino acidsequence identity withamajor portion oftheasubunit ofthesoluble NAD+-reducing hydrogenase fromAkaligenes eutrophus. Inparticular, there arethree segments ofhigh sequence similarity (70-88%) between thetwoproteins which correspond tothethree ligand-binding sites. TheNADH:ubiquinone oxidoreductase orrotenone-sensitive" @default.
- W2187105048 created "2016-06-24" @default.
- W2187105048 creator A5061536209 @default.
- W2187105048 date "1991-01-01" @default.
- W2187105048 modified "2023-09-24" @default.
- W2187105048 title "cDNA-derived aminoacidsequence oftheNADH-binding 51-kDa subunit ofthebovine respiratory NADH dehydrogenase reveals striking similarities toabacterial NAD+-reducing hydrogenase (Akaligenes eutrophus/mRNA levels indssues/human genonic sequences)" @default.
- W2187105048 cites W588812189 @default.
- W2187105048 hasPublicationYear "1991" @default.
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