Cytoenzymology and Isozymes of Cultured Cells

Melivick, P.J.

doi:10.1016/s0079-6336(71)80010-4

Cited by 4 publications

(1 citation statement)

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“…The significance of these observations of isozymes in breast fluid samples awaits the investigation of many more samples. A diagnostic potential would be imminent if it could be established that differing isozyme patterns in a physiologic or pathologic state are conformable (32,35,47), and whether alterations in isozymes are due to variations in rates of their synthesis or to activation from inactive preexisting protein. To this latter point, looking into the future, two-dimensional electrophoretic analysis may play an important part in establishing the antigeneity to catalytic relationship of an isozyme by subsequent staining of gels to electrophoresis (28,36,60).…”

Section: Isozymes and Their Role In Cancermentioning

confidence: 99%

Contributions of Histochemistry to the Development of the Proteolytic Enzyme Detection System in Diagnostic Medicine

Smith

1983

J Histochem Cytochem.

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Section: Isozymes and Their Role In Cancermentioning

confidence: 99%

Contributions of Histochemistry to the Development of the Proteolytic Enzyme Detection System in Diagnostic Medicine

Smith

1983

J Histochem Cytochem.

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Succinate dehydrogenase activity in cultured human skin fibroblasts and amniotic fluid cells

Hansen

Andersen

1983

Histochemistry

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Through a methodological evaluation, reliable histochemical and biochemical methods for succinate dehydrogenase activity in cultured human skin fibroblasts and amniotic fluid cells were developed. The histochemical method includes a cleaning of the cultured cells in 1 mM malonate in 0.9% NaCl, air-drying and fixation in acetone (5 min at -20 degrees C), coating of cells with CoQ10 (0.2 mg/ml in ether/acetone) and incubation for 1 h at 37 degrees C in 50 mM succinate and 0.5 mg/ml Nitro BT in 200 mM phosphate buffer, pH 7.6 PMS as an intermediate electron carrier was found inferior to exogenous CoQ10. Both types of cells exhibit equal activity. In the biochemical method homogenizing was performed in 50 mM Tris-HCl buffer, pH 7.5, and 200 mM sucrose. The standard incubation was 2.0 mM INT and 10 mM succinate in 10 mM Tris-HCl buffer, pH 7.5 for 1 h at 37 degrees C. The apparent Km values for INT and succinate were estimated to 0.39 mM and 0.13 mM, respectively, while I0.5 for malonate was 0.46 mM. Activity in amniotic fluid cells was 18.1 pkat/mg protein and in human skin fibroblasts 20.3 pkat/mg protein. Specificity of the methods was tested by use of a Chinese hamster fibroblast strain B9 known to be succinate dehydrogenase deficient in addition to various control experiments. Congruent results were obtained with the two methods.

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Histochemical assessment of nuclear protein content and enzyme activity in confluent nonarrested and low-serum arrested WI-38 fibroblasts at mid and late population doubling levels

Phillips

Docherty

Mitchell

1982

Mechanisms of Ageing and Development

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Cytoenzymology and Isozymes of Cultured Cells

Cited by 4 publications

References 289 publications

Contributions of Histochemistry to the Development of the Proteolytic Enzyme Detection System in Diagnostic Medicine

Contributions of Histochemistry to the Development of the Proteolytic Enzyme Detection System in Diagnostic Medicine

Succinate dehydrogenase activity in cultured human skin fibroblasts and amniotic fluid cells

Histochemical assessment of nuclear protein content and enzyme activity in confluent nonarrested and low-serum arrested WI-38 fibroblasts at mid and late population doubling levels

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