Miyanaga M, Sugimoto H, Komoda T, Nosjean O, Honma K, Nemoto K, Sato T
Division of Clinical Chemistry, Niigata Cancer Center Hospital, Japan.
Enzyme Protein. 1996;49(5-6):313-20. doi: 10.1159/000468641.
A variant alkaline phosphatase (ALP), with heat-sensitivity characteristics similar to that of the bone type, was found in the serum of a patient suffering from lung cancer. In disc polyacrylamide gel electrophoretic studies most of this enzyme had migrated to the region corresponding to liver ALP, with the remainder affecting bone ALP. Like kidney ALP, this ALP was markedly inhibited by 0.5 mmol/l L-cysteine. The K(m) of this ALP for p-nitrophenylphosphate was 0.39 mmol/l, similar to that of kidney ALP. The sugar moiety of this enzyme bore greater resemblance to that of kidney ALP than liver or bone ALP. However, immunoprecipitation of this particular ALP was strong with a monoclonal antibody against liver ALP and moderate with an antibody against bone ALP.
在一名肺癌患者的血清中发现了一种变异碱性磷酸酶（ALP），其热敏感性特征与骨型碱性磷酸酶相似。在圆盘聚丙烯酰胺凝胶电泳研究中，这种酶的大部分迁移到了对应于肝ALP的区域，其余部分影响骨ALP。与肾ALP一样，这种ALP被0.5 mmol/L的L-半胱氨酸显著抑制。这种ALP对磷酸对硝基苯酯的K(m)为0.39 mmol/L，与肾ALP相似。这种酶的糖部分与肾ALP的糖部分比与肝或骨ALP的糖部分更相似。然而，这种特定的ALP与抗肝ALP单克隆抗体的免疫沉淀反应强烈，与抗骨ALP抗体的免疫沉淀反应中等。
