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Size-exclusion chromatography of WT and I16G β-tryptase zymogens and proteases. WT β-tryptase forms tetramers after activation and pro-domain removal by EK in the presence of 0.5 mg/ml heparin. WT tetramer had an Ve of 13.0 ml on an S200GL column in SEC buffer. Following identical pro-domain removal by EK with heparin, I16G β-tryptase has a Ve of 15.0 ml in SEC buffer, which is essentially identical to that observed for zymogens of WT and I16G β-tryptase.
