Abstract
An acid proteinase has been detected in culture supernate of the 9.2.27 murine hybridoma. This enzyme extensively degrades albumin and transferrin during short incubations at pH 3 and below. Limited proteolysis of the 9.2.27 IgG2a appears to occur in the culture supernate. Proteolysis is enhanced at low pH in the presence of urea or 1 M acetic acid. The proteinase activity accumulates in continuous perfusion, total cell recycle cultures, beginning during exponential growth of the hybridoma. It is destroyed by boiling and blocked by pepstatin, but not by inhibitors of cysteine or serine proteinases or by EDTA. The low pH optimum may distinguish this enzyme from the known rat and mouse aspartic acid proteinases including cathepsin D and cathepsin E.
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A preliminary report of these findings was presented at the 196th National Meeting, American Chemical Society, Los Angeles, September 25–30, 1988; paper #140, Division of Microbial and Biochemical Technology.
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Karl, D.W., Donovan, M. & Flickinger, M.C. A novel acid proteinase relased by hybridoma cells. Cytotechnology 3, 157–169 (1990). https://doi.org/10.1007/BF00143678
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DOI: https://doi.org/10.1007/BF00143678