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Studies on pyruvate carboxylase from cultured human fibroblasts and amniotic fluid cells
Author(s) -
Hansen Torben L.,
Christensen Ernst
Publication year - 1979
Publication title -
journal of inherited metabolic disease
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 102
eISSN - 1573-2665
pISSN - 0141-8955
DOI - 10.1007/bf01799070
Subject(s) - amniotic fluid , pyruvate carboxylase , human genetics , metabolic disease , biology , amnion , andrology , biochemistry , chemistry , medicine , endocrinology , fetus , pregnancy , enzyme , genetics , gene
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.