نتایج جستجو برای: cytochrome oxidase

تعداد نتایج: 89535  

2002
GERA D. EYTAN GOTTFRIED SCHATZ

Cytochrome c oxidase from bakers’ yeast contains three mitochondrially made subunits (I to III) which are relatively hydrophobic and four cytoplasmically made subunits (IV to VII) which are relatively hydrophilic (Mason. T. L., Poyton, R. O., Wharton, D. C., and Schatz, G. (1973) J. Biol. Chem. 248, 1346-1354 and Poyton, R. O., and Schatz, G. (1975) J. Biol. Chem. 250, 752-761. In order to expl...

Journal: :Journal of Histochemistry & Cytochemistry 1975

2003
THOMAS C. DETWILER REGINALD H. GARRETT

The effects of digitonin and tocopherol on bovine heart reduced diphosphopyridine nucleotideand succinate-cytochrome c reductases and cytochrome c oxidase have been studied with the following results. 1. Low concentrations of digitonin stimulate succinateand DPNH-cytochrome c reductase and cytochrome c oxidase. Higher concentrations of digitonin completely inhibit cytochrome c reductases, while...

Journal: :Journal of Biological Chemistry 1965

Journal: :The Journal of Cell Biology 1967
Carl Schnaitman V. Gene Erwin John W. Greenawalt

Controlled osmotic lysis (water-washing) of rat liver mitochondria results in a mixed population of small vesicles derived mainly from the outer mitochondrial membrane and of larger bodies containing a few cristae derived from the inner membrane. These elements have been separated on Ficoll and sucrose gradients. The small vesicles were rich in monoamine oxidase, and the large bodies were rich ...

Journal: :The Journal of biological chemistry 1997
N S Chandel G R Budinger S H Choe P T Schumacker

We previously reported that hepatocytes exhibit a reversible suppression of respiration during prolonged hypoxia (PO2 = 20 torr for 3-5 h). Also, isolated bovine heart cytochrome c oxidase undergoes a reversible decrease in apparent Vmax when incubated under similar conditions. This study sought to link the hypoxia-induced changes in cytochrome oxidase to the inhibition of respiration seen in i...

Journal: :The Journal of biological chemistry 1963
S J COOPERSTEIN

Recent studies on the chemical nature of cytochrome oxidase (cytochrome c :02 oxidoreductase, EC 1.9.3.1) have been concerned largely with the structure of its iron-porphyrin prosthetic group (cj. (l)), the importance of copper as an integral component of the enzyme (e.g. (2-5)), and the possible role of a lipid factor (e.g. (6-8)). By contrast, little work has been done on the nature of the fu...

Journal: :The Journal of biological chemistry 1965
A P MARTIN G E DOYLE E STOTZ

Since the pioneer studies of Keilin and Hartree (l), considerable evidence has accumulated indicating that cytochrome c oxidase contains two heme moieties that react differently; hence the designation cytochrome U-Q. Reasons for this designat.ion include kinetic studies that show (a) differences in the rate of reduction and oxidation of cytochrome c oxidase measured at the a versus y absorption...

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