Abstract
Alkaline phosphatase (ALP) components in 8 cell lines of HeLa were examined. Line to line heterogeneity in ALP expression was observed using the criteria of electrophoretic mobility before and after neuraminidase treatment, heat stability,l-phenylanine inhibition, and reactivity against antiplacental ALP antiserum. Six lines contained a placentallike ALP isozyme and varying amounts of a liverlike ALP isozyme. One line contained a liverlike ALP isozyme only. One line contained a new ALP form which was clearly distinguished from the placental, liver, bone, and intestinal ALPs. Thus, derepression of the placental ALPstructural locus appeared to have occurred in 6 of the 8 lines. However, where expressed, the placentallike ALP varied electrophoretically from line to line, and in only one case was the mobility identical to that of a common placental ALP phenotype. This phenotypic heterogeneity of the “derepressed” placentallike ALP contrasts markedly with the phenotypic stability of other enzymes expressed in HeLa cells.
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Benham, F.J., Povey, M.S. & Harris, H. Heterogeneity of alkaline phosphatases in different HeLa lines. Somat Cell Mol Genet 4, 13–25 (1978). https://doi.org/10.1007/BF01546490
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DOI: https://doi.org/10.1007/BF01546490