Kässner G, Neupert G, Scheibe R, Wenzel K W
University of Leipzig, School of Medicine, Institute of Biochemistry, Germany.
Exp Pathol. 1991;43(1-2):51-6. doi: 10.1016/s0232-1513(11)80142-8.
In cultured epithelial cells of rat liver the isoenzyme patterns of pyruvate kinase, lactate dehydrogenase and alkaline phosphatase were studied and compared with those of freshly isolated parenchymal and non-parenchymal liver cells. In all epithelial cell lines pyruvate kinase was not activated by fructose 1,6-bisphosphate, suggesting the absence of the L-isoenzyme. Cell lines derived from livers of newborn rats expressed LDH-4 and -5, whereas cell lines developed from fetal rat livers contained all 5 lactate dehydrogenase isoenzymes. In the latter case the pattern was found to depend on the state of confluence. All cell lines exhibited only a single alkaline phosphatase form, however, differences were found with respect to electrophoretic mobility.
在大鼠肝脏的培养上皮细胞中,研究了丙酮酸激酶、乳酸脱氢酶和碱性磷酸酶的同工酶模式,并与新鲜分离的实质肝细胞和非实质肝细胞的同工酶模式进行了比较。在所有上皮细胞系中,丙酮酸激酶未被1,6-二磷酸果糖激活,提示不存在L-同工酶。新生大鼠肝脏来源的细胞系表达LDH-4和-5,而胎鼠肝脏来源的细胞系含有所有5种乳酸脱氢酶同工酶。在后一种情况下,发现该模式取决于汇合状态。所有细胞系仅表现出单一的碱性磷酸酶形式,然而,在电泳迁移率方面发现了差异。