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Difference between revisions of "Ziegler 1962 Arch Biochem Biophys"

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{{Publication
{{Publication
|title=Ziegler DM, Doeg KA (1962) Studies on the electron transport system XLIII. The isolation of a succinic-coenzyme Q reductase from beef heart mitochondria. Arch Biochem Biophys 97: 41-50. ย 
|title=Ziegler DM, Doeg KA (1962) Studies on the electron transport system XLIII. The isolation of a succinic-coenzyme Q reductase from beef heart mitochondria. Arch Biochem Biophys 97: 41-50.
|info=[http://www.sciencedirect.com/science/journal/00039861/97/1 ScienceDirect]
|info=[http://www.sciencedirect.com/science/journal/00039861/97/1 ScienceDirect]
|authors=Ziegler DM, Doeg KA
|authors=Ziegler DM, Doeg KA
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A rapid spectrophotometric method for measuring the succinic-CoQ reductase activity of mitochondria and of the purified enzyme is described.
A rapid spectrophotometric method for measuring the succinic-CoQ reductase activity of mitochondria and of the purified enzyme is described.
|keywords=succinic-coenzyme Q reductase, flavine content
|keywords=Succinic-coenzyme Q reductase, Flavine content, Beef heart mitochondria
}}
}}
{{Labeling
{{Labeling
|organism=Other Mammal
|organism=Mammals
|tissues=Cardiac muscle
|tissues=Cardiac muscle
|preparations=Isolated Mitochondria
|preparations=Isolated Mitochondria

Revision as of 12:28, 13 February 2013

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Ziegler DM, Doeg KA (1962) Studies on the electron transport system XLIII. The isolation of a succinic-coenzyme Q reductase from beef heart mitochondria. Arch Biochem Biophys 97: 41-50.

ยป ScienceDirect

Ziegler DM, Doeg KA (1962) Arch Biochem Biophys

Abstract: The isolation of the succinic-CoQ reductase from beef heart mitochondria is described. The flavine content of the preparation is 4.8 mฮผmoles/mg. protein, and all of the flavine is extracted by acid only after the preparation is treated with proteolytic enzymes. The preparation also contains non-heme iron, lipid, and protoheme, and the last mentioned is present in an amount equivalent to the flavine. Based on the flavine or heme content, the minimum molecular weight in terms of protein is 210,000. The heme present in the purified enzyme is not reduced by succinate, which makes its participation as an electron carrier in the reactions catalyzed by the enzyme very unlikely.

A rapid spectrophotometric method for measuring the succinic-CoQ reductase activity of mitochondria and of the purified enzyme is described. โ€ข Keywords: Succinic-coenzyme Q reductase, Flavine content, Beef heart mitochondria


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Organism: Mammals"Mammals" is not in the list (Human, Pig, Mouse, Rat, Guinea pig, Bovines, Horse, Dog, Rabbit, Cat, ...) of allowed values for the "Mammal and model" property.  Tissue;cell: Cardiac muscle"Cardiac muscle" is not in the list (Heart, Skeletal muscle, Nervous system, Liver, Kidney, Lung;gill, Islet cell;pancreas;thymus, Endothelial;epithelial;mesothelial cell, Blood cells, Fat, ...) of allowed values for the "Tissue and cell" property.  Preparation: Isolated Mitochondria"Isolated Mitochondria" is not in the list (Intact organism, Intact organ, Permeabilized cells, Permeabilized tissue, Homogenate, Isolated mitochondria, SMP, Chloroplasts, Enzyme, Oxidase;biochemical oxidation, ...) of allowed values for the "Preparation" property.  Enzyme: Complex II; Succinate Dehydrogenase"Complex II; Succinate Dehydrogenase" is not in the list (Adenine nucleotide translocase, Complex I, Complex II;succinate dehydrogenase, Complex III, Complex IV;cytochrome c oxidase, Complex V;ATP synthase, Inner mt-membrane transporter, Marker enzyme, Supercomplex, TCA cycle and matrix dehydrogenases, ...) of allowed values for the "Enzyme" property. 



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