Abstract
A soluble proteinaceous invertase inhibitor was purified from tubers of cv. Provita. N-terminal amino acid sequencing of the purified protein indicated that the invertase inhibitor was a member of a family of small tuber proteins known as Kunitz-type protease inhibitors. The purified protein was completely inhibitory to soluble tuber invertase at quantities that did not inhibit trypsin. Based on amino acid sequence information of invertase inhibitor protein, seven candidate cDNA clones were identified in libraries of Provita and Saturna tubers. The candidate cDNA sequences differed from each other between 2% and 5%, having several non-conservative amino acid substitutions when compared with sequence related protease inhibitors. The results suggest invertase as an alternative target of tuber “protease” inhibitors.
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