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Studies on pyruvate carboxylase from cultured human fibroblasts and amniotic fluid cells

1979; Springer Science+Business Media; Volume: 2; Issue: 2 Linguagem: Inglês

10.1007/bf01799070

1573-2665

Torben Lindskov Hansen, Ernst Christensen,

Amino Acid Enzymes and Metabolism

Abstract The properties of pyruvate carboxylase in cultured human fibroblasts were investigated. A pH optimum around pH 7.6 was found in Tris buffer at 37°C. The apparent K m for pyruvate and bicarbonate were 0.22 mmol/l and 2.1 mmol/l respectively. The activity of the crude homogenate was most stable at room temperature. The major end product was identified as citric acid during the assay conditions used. During growth the specific activity increased from 0.5 to 2 nmol/min per mg protein. The activity of pyruvate carboxylase in the crude homogenate from cultured human fibroblasts was 0.76±0.12 nmol/min per mg protein, while the activity in cultured amniotic fluid cells was 0.66±0.17 nmol/min per mg protein, suggesting the possibility of prenatal diagnosis of pyruvate carboxylase deficiency.