Gobeev V N, Khripach L V
Vopr Med Khim. 1976 Nov-Dec;22(6):798-804.
In hepatomas of various malignancy contrary to normal and regenerating liver tissue a considerable part of hexokinase (HK) activity was bound with mitochondria. The HK activity, estimated in nuclei, microsomes and apparently in cytoplasma membranes, was due to contamination with mitochondrial fraction. High specific activity of HK in mitochondria of tumors might be responsible for the increased glycolysis, when these organelle preparations were added to the soluble fraction of cells. The HK of tumors was extracted from the preparations by alternative pathways. Reversible binding of some part of the enzyme with mitochondria was regulated by concentration of metabolites (ATP and G6P) similarly to the bound HK from normal tissues (brain, retina). At the same time the other part of unregulated HK activity (isozyme I only) was found in hepatomas to be intercalated into lipoprotein membranes; it was not controlled by metabolites.
与正常和再生肝组织相反，在各种恶性程度的肝癌中，相当一部分己糖激酶（HK）活性与线粒体结合。在细胞核、微粒体以及明显在细胞质膜中估计的HK活性，是由于线粒体部分的污染所致。当将这些细胞器制剂添加到细胞的可溶部分时，肿瘤线粒体中HK的高比活性可能是糖酵解增加的原因。肿瘤的HK是通过替代途径从制剂中提取的。该酶的一部分与线粒体的可逆结合受代谢物（ATP和G6P）浓度的调节，这与正常组织（脑、视网膜）中结合的HK类似。同时，在肝癌中发现不受调节的HK活性的另一部分（仅同工酶I）插入脂蛋白膜中；它不受代谢物的控制。
