Abstract
The human hepatoma cell line SK-HEP-1 has been shown by radioimmunoelectrophoresis to synthesize and secrete a protein which coprecipitates with human α1-antitrypsin. This protein was indistinguishable from serum α1-antitrypsin in terms of electrophoretic mobility, apparent subunit molecular weight (47,000), and binding to concanavalin-A. The protein identified as α1-antitrypsin (α1AT) was secreted by seven clones derived from SK-HEP-1 and by twelve out of eighteen hybrid clones derived from the fusion of SK-HEP-1 with mouse RAG cells. There was no correlation between the expression of α1AT and that of human enzymes assigned to sixteen different autosomes. There was an imperfect correlation between the expression of α1AT and of the two chromosome 9 marker enzymes AK1 and AK3 (two discordant clones).
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Turner, B.M., Turner, V.S. Secretion ofα 1-antitrypsin by an established human hepatoma cell line and by human/mouse hybrids. Somat Cell Mol Genet 6, 1–14 (1980). https://doi.org/10.1007/BF01538692
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DOI: https://doi.org/10.1007/BF01538692