Volek V
Acta Univ Carol Med Monogr. 1977(78 Pt 2):51-4.
Lactate dehydrogenase (LDH, E.C. 1.1.1.27) activity was studied in an experimental model (the liver bile of cholecystectomized patients and of rats) by electrophoretic separation on agar gel. The prevalence of the liver LDH5 isoenzyme in bile obtained in this manner is the proof that this fraction is secreted by the liver. The experimental conclusions are supported by the author's own clinical observations of prevalence of the cathodic isocomponents LDH4 and LDH5 in serum, as an indicator of cholestasis in conditions characterized by bile duct obstruction.
通过在琼脂凝胶上进行电泳分离,在一个实验模型(胆囊切除患者和大鼠的肝胆汁)中研究了乳酸脱氢酶(LDH,E.C. 1.1.1.27)的活性。以这种方式获得的胆汁中肝脏LDH5同工酶的优势证明了该组分是由肝脏分泌的。作者自己对血清中阴极等成分LDH4和LDH5的普遍性的临床观察支持了这些实验结论,将其作为胆管梗阻所特征的情况下胆汁淤积的一个指标。