Neumann H, Klein E, Hauck-Granoth R, Yachnin S, Ben-Bassat H
Proc Natl Acad Sci U S A. 1976 May;73(5):1432-6. doi: 10.1073/pnas.73.5.1432.
Alkaline phosphatase [orthophosphoricmonoester phosphohydrolase (alkaline pH optimum), EC 3.1.3.1] purified from a Burkitt lymphoma cell line (Daudi) and Moloney-virus-induced murine leukemia (YAC) showed unique catalytic properties in substrate specificity and inhibition by cysteamine-S-phosphate. It migrated on polyacrylamide gel electrophoresis in a single activity band. Alkaline phosphatase with similar properties was found in several human lymphoblastoid cell lines, in chronic lymphatic leukemic cells, in organs of leukemic mice, and in sera of patients with certain lymphoproliferative disorders.
从伯基特淋巴瘤细胞系(Daudi)和莫洛尼病毒诱导的小鼠白血病(YAC)中纯化得到的碱性磷酸酶[正磷酸单酯磷酸水解酶(最适pH为碱性),EC 3.1.3.1]在底物特异性和被半胱胺 - S - 磷酸抑制方面表现出独特的催化特性。它在聚丙烯酰胺凝胶电泳中迁移至单一活性条带。在几种人淋巴母细胞系、慢性淋巴细胞白血病细胞、白血病小鼠的器官以及某些淋巴增殖性疾病患者的血清中发现了具有相似特性的碱性磷酸酶。