Volumetric and Gravimetric Analytical Methods of Organic Compounds

Smith, Walter T.; Wagner, William F.; Patterson, John M.

doi:10.1021/ac60161a019

Cited by 2 publications

(1 citation statement)

References 64 publications

(69 reference statements)

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“…The activity thus measured was the same as that assayed after sonication at 0-20C for 10min [with maximum power on the MSE Ultrasonic (disintegrator) Model 150W], but activation by Triton was more convenient where several fractions required assay. Cytochrome oxidase was assayed by observing the re-oxidation of reduced cytochrome c, as described by Smith (1960), with fraction samples clarified by sonication or by treatment with Triton X-100 as described above. D-Amino acid oxidase was assayed by measuring the pyruvate formed aerobically from D-alanine.…”

Section: Enzyme Assaysmentioning

confidence: 99%

The subcellular distribution of rat liver serine-pyruvate aminotransferase

Rowsell¹,

Al-Naama²,

Benett³

1982

Biochemical Journal

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1. The subcellular distribution of L-serine-pyruvate aminotransferase activity in rat liver was investigated. About 80% was recovered from cell-free homogenates in a 'total-particles' fraction and the remainder in the cytosol. 2. Subfractionation of the particles by differential sedimentation and on sucrose density gradients showed a distribution for serine-pyruvate aminotransferase activity closely matching that observed for mitochondrial marker enzymes. 3. A study of the solubilization of enzymes from combined subcellular particles by digitonin at various concentrations also indicated a common subcellular location for serine-pyruvate aminotransferase and established mitochondrial enzymes. 4. The increase in liver serine-pyruvate amino-transferase activity induced by glucagon injection was accounted for as an increased mitochondrial activity.

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Section: Enzyme Assaysmentioning

confidence: 99%