A human heteroploid epithelial-like cell line, designated as C-SPT, was recovered from one of several lots of human WI-38 fibroblast-like diploid cells that lacked evidence of Regan isozyme in early passages. In later passages with the growth of C-SPT cells, high activity of Regan type of alkaline phosphatase appeared as judged by l-phenylalanine inhibition, heat stability, and immunoelectrophoresis. The C-SPT cells appeared to be the progeny of an unidentified source contaminant rather than of transformed WI-38 cells. Comparative enzymological and immunological studies with HeLa and WISH cells confirmed the presence of Regan type of alkaline phosphatase as a characteristic of HeLa and established its presence in WISH cells. However, the specific activity of Regan isozyme in WISH cells was only 3 to 6% of that in C-SPT cells. The HeLa cells exhibited 33% of C-SPT level on the initial passage level studied, which after further cell passage declined to 8%. A HeLa clone was isolated showing very high activity of non-Regan type of alkaline phosphatase, presumably of “bone” type.

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