Abstract
'Désirée' potato tubers contained about one-half the patatin of 'Kennebec', a typical commercial cultivar. The 'Désirée' patatin, like that of 'Kennebec', copurified with esterase activity, but it consisted of only two major ionic forms and its ability to hydrolyse p-nitrophenyl esters was relatively low. Despite these differences, the esterase of 'Désirée' patatin was quite active toward other substrates. Patatin isoforms, separated by isoelectric focusing, had the same esterase substrate preference as the cultivar-specific patatin from which they were derived.
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