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Abstract
The effect of Mn 2+ and Ca 2+ on the kinetics of the tryptic activation of bovine trypsinogen was studied at pH 7.3 and 36.5°C. For comparison, the rate constants of autolysis and esterolytic activity of trypsin were also determined. It can be concluded that Mn 2+ increases the conversion rate of trypsinogen into trypsin in a 25–40% larger extent than Ca 2+. The manganese(II) ion bond to trypsinogen is supposed to keep the N-terminal part of the zymogen in a better conformation for binding at the primary and secondary binding sites of trypsin.
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