Difference between revisions of "Hatefi 1961 Biochim Biophys Acta"
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{{Publication | {{Publication | ||
|title=Hatefi Y, Haavik AG, Jurtshuk P ( | |title=Hatefi Y, Haavik AG, Jurtshuk P (1961) Studies on the electron transport system XXXI. DPNH-cytochrome c reductase II. Biochim Biophys Acta 52:106-18. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/13905330 PMID: 13905330] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/13905330 PMID: 13905330] | ||
|authors=Hatefi Y, Haavik AG, Jurtshuk P | |authors=Hatefi Y, Haavik AG, Jurtshuk P | ||
|year= | |year=1961 | ||
|journal=Biochim Biophys Acta | |journal=Biochim Biophys Acta | ||
|abstract=A highly active DPNH-cytochrome c reductase has been isolated from beef-heart mitochondria. The best preparations of the enzyme catalyze the reduction by DPNH of approx. 50–60 μmoles cytochrome c/min/mg protein at 38°. The enzymic activity is completely inhibited by Amytal, p-chloromercuriphenyl sulfonate, antimycin A, SN-5949 or 2-nonyl-4-hydroxyquinoline-N-oxide, and is stimulated by EDTA. The preparation contains DPNH flavoprotein, cytochromes b and c1, Coenzyme Q and non-heme iron and is essentially free of succinic-cytochrome c reductase as well as cytochrome oxidase activity. | |abstract=A highly active DPNH-cytochrome c reductase has been isolated from beef-heart mitochondria. The best preparations of the enzyme catalyze the reduction by DPNH of approx. 50–60 μmoles cytochrome c/min/mg protein at 38°. The enzymic activity is completely inhibited by Amytal, p-chloromercuriphenyl sulfonate, antimycin A, SN-5949 or 2-nonyl-4-hydroxyquinoline-N-oxide, and is stimulated by EDTA. The preparation contains DPNH flavoprotein, cytochromes b and c1, Coenzyme Q and non-heme iron and is essentially free of succinic-cytochrome c reductase as well as cytochrome oxidase activity. | ||
|keywords=DPNH-cytochrome c reductase, | |keywords=DPNH-cytochrome c reductase, Beef heart mitochondria | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
|organism= | |organism=Bovines | ||
|tissues= | |tissues=Heart | ||
|preparations=Isolated | |preparations=Isolated mitochondria | ||
|enzymes=Complex IV; | |enzymes=Complex IV;cytochrome c oxidase | ||
| | |topics=Substrate | ||
|couplingstates=ET | |||
|additional=Made history | |additional=Made history | ||
}} | }} | ||
Latest revision as of 14:33, 13 November 2017
| Hatefi Y, Haavik AG, Jurtshuk P (1961) Studies on the electron transport system XXXI. DPNH-cytochrome c reductase II. Biochim Biophys Acta 52:106-18. |
Hatefi Y, Haavik AG, Jurtshuk P (1961) Biochim Biophys Acta
Abstract: A highly active DPNH-cytochrome c reductase has been isolated from beef-heart mitochondria. The best preparations of the enzyme catalyze the reduction by DPNH of approx. 50–60 μmoles cytochrome c/min/mg protein at 38°. The enzymic activity is completely inhibited by Amytal, p-chloromercuriphenyl sulfonate, antimycin A, SN-5949 or 2-nonyl-4-hydroxyquinoline-N-oxide, and is stimulated by EDTA. The preparation contains DPNH flavoprotein, cytochromes b and c1, Coenzyme Q and non-heme iron and is essentially free of succinic-cytochrome c reductase as well as cytochrome oxidase activity. • Keywords: DPNH-cytochrome c reductase, Beef heart mitochondria
Labels:
Organism: Bovines
Tissue;cell: Heart
Preparation: Isolated mitochondria
Enzyme: Complex IV;cytochrome c oxidase
Regulation: Substrate
Coupling state: ET
Made history
