Prowl Lab,Rockefeller University
http://prowl.rockefeller.edu/recipes/sproteas/pepsin.htm
SpecificityCleaves preferentially C-terminal to F,L and E. It does not cleave at V, A or G. Other residues may be cleaved, with very variable rates.
pH optimum2 - 4
StabilityActive in 4 M urea and 3 M guanidine HCl. Enzyme is stable at 60 C. Pepsin is irreversibly inactived at pH > 6.
RecipeDissolve the substate in 10 mM HCl at 1-10 g/l and adjust the pH to 2.0. Add pepsin at 1:100 and incubate for 1 hour at 25 C. Pepsin acts very quickly at room temperature.
Be very careful handling pepsin. If it contaminates a stock solution with 0.1 % TFA, it will remain active.
Konigsberg, W., Goldstein, J. and Hill, R.J. the structure of human haemoglobin VII. The digestion of the beta chain of human haemoglobin with pepsin. J. Biol. Chem. 238(1963)2028-2033.
上一篇：CNBr mapping【Salk Institute】 下一篇：Chazin Lab Protocol for Limited Proteolysis
|
