Intracellular Distribution of Xanthine Oxidase in the Rat Liver

Villela, Gilberto G.; E, Mitidieri; Affonso, Ottília R.

doi:10.1038/1751087a0

Cited by 33 publications

(3 citation statements)

References 4 publications

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“…The distribution of xanthine oxidase likewise appeared to be uninfluenced by alterations in hormonal balance. Most of the cytoplasmic activity was recovered in the supernatant fraction and none was found in the particulate fractions, in accordance with previous findings (Meikleham, Wells, Richert & Westerfeld, 1951;Villela, Mitidieri & Affonso, 1955;Morell, 1955).…”

Section: Discussionsupporting

confidence: 92%

Hormones and liver cytoplasm. 2. Adenosine triphosphatase, glucose 6-phosphatase and xanthine oxidase as affected by hypophysectomy, growth-hormone treatment and adrenalectomy

Reid

O'Neal

Lewin

1956

Biochemical Journal

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Section: Discussionsupporting

confidence: 92%

Hormones and liver cytoplasm. 2. Adenosine triphosphatase, glucose 6-phosphatase and xanthine oxidase as affected by hypophysectomy, growth-hormone treatment and adrenalectomy

Reid

O'Neal

Lewin

1956

Biochemical Journal

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“…Xanthine oxidase is located in the particle-free supernatant (Schein & Young, 1952;Villela, Mitidieri & Affonso, 1955). Fig.…”

Section: Subcellular Fraction Supernatant + Microsomes Protein Fractimentioning

confidence: 99%

Oxidation of reduced glutathione by subcellular fractions of rat liver

Christophersen¹

1966

Biochemical Journal

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1. A new method was used to diminish the autoxidation of GSH. 2. The oxidation of GSH by liver homogenates was studied with regard to concentration of homogenate, concentration of GSH, time, pH and anaerobiosis. 3. GSH was oxidized by recombinations of the supernatant with microsomes and with mitochondria. Each fraction alone caused little oxidation. 4. Proteins in the supernatant were required to obtain the effect, and low-molecular-weight compounds in the same fraction increased its effect. 5. GSH diminished the formation of malonaldehyde in homogenates. 6. GSH prevented a stimulating effect of the supernatant on the formation of malonaldehyde in microsomes and in mitochondria. 7. The malonaldehyde formation in microsomes together with the supernatant did not start until the concentration of endogenous low-molecular-weight thiols had decreased to a low level. 8. It is suggested that part of the oxidation of GSH in homogenates is coupled to a mechanism that counteracts the peroxidation of membrane lipids.

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“…The evidence previously presented that GSH oxidation by rat liver homogenate may depend on xanthine oxidase acting on endogenous xanthine or hypoxanthine (Jocelyn, 1970) appeared incompatible with a report that the oxidation is prevented by removal of microsomes (Christophersen, 1966), since xanthine oxidase is exclusively a supernatant enzyme (Villela, Mitidieri & Affonso, 1955).…”

mentioning

confidence: 87%

The function of subcellular fractions in the oxidation of glutathione in rat liver homogenate

Jocelyn

1970

Biochemical Journal

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1. The aerobic loss of GSH added to the supernatant fraction from rat liver is much increased by including the microsome fraction, which both inhibits the concurrent reduction of the GSSG formed and also augments the net oxidation rate. 2. Oxidation occurs with a mixture of dialysed supernatant and a protein-free filtrate; the latter is replaceable by hypoxanthine and the former by xanthine oxidase, whereas fractions lacking this enzyme give no oxidation. 3. In all these instances augmentation occurs with microsomes, with fractions having urate oxidase activity and with the purified enzyme; uric acid and microsomes alone also support the oxidation. 4. Evidence implicating additional protein factors is discussed. 5. It is suggested that GSH oxidation by homogenate is linked through glutathione peroxidase to the reaction of endogenous substrate with supernatant xanthine oxidase and of the uric acid formed with peroxisomal urate oxidase.

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Intracellular Distribution of Xanthine Oxidase in the Rat Liver

Cited by 33 publications

References 4 publications

Hormones and liver cytoplasm. 2. Adenosine triphosphatase, glucose 6-phosphatase and xanthine oxidase as affected by hypophysectomy, growth-hormone treatment and adrenalectomy

Hormones and liver cytoplasm. 2. Adenosine triphosphatase, glucose 6-phosphatase and xanthine oxidase as affected by hypophysectomy, growth-hormone treatment and adrenalectomy

Oxidation of reduced glutathione by subcellular fractions of rat liver

The function of subcellular fractions in the oxidation of glutathione in rat liver homogenate

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