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Monoclonal antibodies block the bromelain‐mediated release of human placental alkaline phosphatase from cultured cancer cells
Author(s) -
Jemmerson Ronald,
Millan Jose Luis,
Klier F.George,
Fishman William H.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80542-1
Subject(s) - placental alkaline phosphatase , bromelain , monoclonal antibody , alkaline phosphatase , proteolysis , cleavage (geology) , antibody , protease , microbiology and biotechnology , chemistry , phosphatase , biochemistry , monoclonal , enzyme , biology , immunology , paleontology , fracture (geology)
Certain monoclonal antibodies (mAbs) to human placental alkaline phosphatase (PLAP) block bromelain cleavage of a 2‐kDa segment from each of the two polypeptide chains of PLAP. These mAbs also prevent the release of PLAP from cultured cancer cell surfaces by bromelain. Such proteolysis‐blocking mAbs serve as tools to specifically modify the molecular topography of cell surfaces by protease treatment.