Monoclonal antibodies block the bromelain‐mediated release of human placental alkaline phosphatase from cultured cancer cells
- 7 January 1985
- journal article
- Published by Wiley in FEBS Letters
- Vol. 179 (2), 316-320
- https://doi.org/10.1016/0014-5793(85)80542-1
Abstract
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.Keywords
This publication has 11 references indexed in Scilit:
- Monoclonal antibodies block the trypsin cleavage site on human placental alkaline phosphataseFEBS Letters, 1984
- Antigenic determinants of human placental and testicular placental‐like alkaline phosphatases as mapped by monoclonal antibodiesEuropean Journal of Biochemistry, 1983
- Measurement of biosynthetic rates and intracellular transit times for a cell-surface membrane glycoprotein, alkaline phosphatase in HeLa cellsAnalytical Biochemistry, 1983
- Differential release of membrane-bound alkaline phosphatase isoenzymes from tumor cells by bromelainJournal of Biochemical and Biophysical Methods, 1980
- Release of alkaline phosphatase from membranes by a phosphatidylinositol-specific phospholipase C.Biochemical Journal, 1977
- Purification and partial characterization of two genetic variants of placental alkaline phosphataseBiochemical Genetics, 1976
- CHARACTERIZATION OF TWO HELA SUBLINES: TCRC-1 PRODUCES REGAN ISOENZYME AND TCRC-2, NON-REGAN ISOENZYMEThe Journal of cell biology, 1974
- Exposed protein on the intact human erythrocyteBiochemistry, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Preparation of Iodine-131 Labelled Human Growth Hormone of High Specific ActivityNature, 1962