Kappa-elastin peptides, obtained from insoluble elastin by organo-alkaline hydrolysis, were fractioned by gel filtration on Biogel agarose. Rates of hydrolysis by pancreatic and leukocyte elastases of the fractions were measured using a conductometric method. Kinetics obey to Michaelis-Menten model for both substrates and enzymes. KM and Vmax values derived from Lineweaver-Burk plots indicate that, if KM remains quite constant, differences were observed in catalytic rates. The kcat values decreased with molecular-weight, the high-molecular-weight kappa-elastin peptides being hydrolyzed 3 to 5 times faster than the low-molecular-weight ones. Apparent differences between potentiometric (pH-Stat) and conductometric results were discussed, in relation with buffer capacity of soluble and insoluble elastins.
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