Mechanism on how trypsin detaches the adhered cells
Answers
Trypsin is a member of the serine protease family. It cleaves peptides onthe C-terminal side of Lysine or Arginine. Trypsin is by far the most commonly used enzyme in tissue culture to release the adherent cells from culture vessel surface and/or to disaggregate tissue into single cell suspension.
Cell-cell and cell-matrix interaction depends on the adhesion molecules, which in turn, relies on the presence of calcium. Tissue culture media contains calcium and magnesium ions, fetal bovine serum contains proteins that are trypsin inhibitors. Both Mg2+ and Ca2+ inhibit trypsin.
To weaken the function of adhesion molecules, EDTA is frequently included in the trypsin solution for its function as divalent cations chelator.
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