Prowl Lab,Rockefeller University
http://prowl.rockefeller.edu/recipes/sproteas/endoarg.htm
Specificity
Cleaves C-terminal to R. Some R-X bonds are resistant, but the systematics are unknown. Some cleavage at K-X bonds has also been observed.
pH optimum
7.5 - 8.5
Stability
Enzyme remains active in 0.1% SDS, but activity drops with time. Enzyme is denatured by 4 M urea. Purified enzyme autolyzes to form a smaller, also active form of the enzyme.
Recipe
Dissolve the substrate in 1% ammonium bicarbonate. Add the enzyme at 1:50 and incubate for 8 hours at 37 C.
Poncz, L. and Dearborn, D.G. The resistance to tryptic hydrolysis of peptide bonds adjacent to N,N-dimethyllysyl residues. J. Biol. Chem. 258(1983)1844-1850.
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