In the presence of a diphosphate substrate or substrate analogue, rabbit muscle aldolase undergoes a limited proteolysis by chymotrypsin. The sole products are an enzyme with modified catalytic properties and two hexapeptides removed from the COOH terminus of the α and β subunits, respectively. The enzyme product has catalytic properties similar to those of aldolase modified by carboxypeptidase A in that it retains full activity with fructose 1-phosphate as substrate but has lost 95% of the original activity with fructose 1,6-diphosphate as substrate. The hexapeptides have the structures Ile-Ser-Asn-His-Ala-Tyr (α subunit) and Ile-Ser-Asp-His-Ala-Tyr (β subunit) and are produced in approximately equal amounts from aldolase preparations obtained from adult animals.
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Midelfort et al. (1972) studied this question.