| http://purl.uniprot.org/citations/3891338 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/3891338 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/3891338 | http://www.w3.org/2000/01/rdf-schema#comment | "The nicotinamide nucleotide transhydrogenase of Escherichia coli has been purified from cytoplasmic membranes by pre-extraction of the membranes with sodium cholate and Triton X-100, solubilization of the enzyme with sodium deoxycholate in the presence of 1 M potassium chloride, and centrifugation through a 1.1 M sucrose solution. The purified enzyme consists of two subunits, alpha and beta, of apparent Mr 50000 and 47000. During transhydrogenation between NADPH and 3-acetylpyridine adenine dinucleotide by both the purified enzyme reconstituted into liposomes and the membrane-bound enzyme, a pH gradient is established across the membrane as indicated by the quenching of the fluorescence of 9-aminoacridine. Treatment of transhydrogenase with N,N'-dicyclohexylcarbodiimide results in an inhibition of proton pump activity and transhydrogenation, suggesting that proton translocation and catalytic activities are obligatory linked. NADH protected the enzyme against inhibition by N,N'-dicyclohexylcarbodiimide, while NADP, and to a lesser extent NADPH, appeared to increase the rate of inhibition. [14C]Dicyclohexylcarbodiimide preferentially labelled the 50000-Mr subunit of the transhydrogenase enzyme. The presence of an allosteric binding site which reacts with NADH, but not with reduced 3-acetylpyridine adenine dinucleotide, has been demonstrated."xsd:string |
| http://purl.uniprot.org/citations/3891338 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1985.tb08955.x"xsd:string |
| http://purl.uniprot.org/citations/3891338 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1985.tb08955.x"xsd:string |
| http://purl.uniprot.org/citations/3891338 | http://purl.uniprot.org/core/author | "Bragg P.D."xsd:string |
| http://purl.uniprot.org/citations/3891338 | http://purl.uniprot.org/core/author | "Clarke D.M."xsd:string |
| http://purl.uniprot.org/citations/3891338 | http://purl.uniprot.org/core/date | "1985"xsd:gYear |
| http://purl.uniprot.org/citations/3891338 | http://purl.uniprot.org/core/name | "Eur J Biochem"xsd:string |
| http://purl.uniprot.org/citations/3891338 | http://purl.uniprot.org/core/pages | "517-523"xsd:string |
| http://purl.uniprot.org/citations/3891338 | http://purl.uniprot.org/core/title | "Purification and properties of reconstitutively active nicotinamide nucleotide transhydrogenase of Escherichia coli."xsd:string |
| http://purl.uniprot.org/citations/3891338 | http://purl.uniprot.org/core/volume | "149"xsd:string |
| http://purl.uniprot.org/citations/3891338 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3891338 |
| http://purl.uniprot.org/citations/3891338 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3891338 |
| http://purl.uniprot.org/citations/3891338 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/3891338 |
| http://purl.uniprot.org/citations/3891338 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/3891338 |
| http://purl.uniprot.org/enzyme/7.1.1.1 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/3891338 |
| http://purl.uniprot.org/uniprot/P0AB67#attribution-986D23E618CF9B7FF86256CE712B151E | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/3891338 |
| http://purl.uniprot.org/uniprot/P07001#attribution-986D23E618CF9B7FF86256CE712B151E | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/3891338 |