Hansen T L, Christensen E
J Inherit Metab Dis. 1980;2(2):23-8. doi: 10.1007/BF01799070.
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 degrees C. The apparent Km 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.
对培养的人成纤维细胞中丙酮酸羧化酶的特性进行了研究。在37℃的Tris缓冲液中发现最适pH约为7.6。丙酮酸和碳酸氢盐的表观Km分别为0.22 mmol/L和2.1 mmol/L。粗匀浆的活性在室温下最稳定。在所使用的测定条件下，主要终产物被鉴定为柠檬酸。在生长过程中，比活性从0.5增加到2 nmol/分钟每毫克蛋白质。培养的人成纤维细胞粗匀浆中丙酮酸羧化酶的活性为0.76±0.12 nmol/分钟每毫克蛋白质，而培养的羊水细胞中的活性为0.66±0.17 nmol/分钟每毫克蛋白质，提示丙酮酸羧化酶缺乏症产前诊断的可能性。
