Abstract
P-glycoprotein (P-gp) plays a fundamental role in multidrug resistance. The quantity of P-gp relates to the degree of drug resistance. A comparison was made between P-gps in mouse and hamster cell lines in both Laemmli and modified Fairbanks gel systems. Both proteins are derived from precursors of similar size that undergo differential N-linked glycosylation. The electrophoretic mobility and the amount of P-gp are remarkably dependent on the conditions of analysis. Notably, boiling P-gp before Laemmli gel elec-trophoresis decreases its mobility by an amount that is equivalent to ≈15 kDa and results in an apparent diminution in the amount of protein. The latter effect can give a false impression concerning the quantity of P-gp in cells.
Original language | English (US) |
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Pages (from-to) | 506-510 |
Number of pages | 5 |
Journal | Journal of the National Cancer Institute |
Volume | 80 |
Issue number | 7 |
DOIs | |
State | Published - Jun 1 1988 |
Externally published | Yes |
ASJC Scopus subject areas
- Oncology
- Cancer Research