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Three protein proteolytic enzyme inhibitors with molecular masses 21, 22, and 23 kDa have been isolated from intact potato tubers (Solanum tuberosum L. cv. Istrinskii). The 21 and 22 kDa proteins denoted as PSPI-21 and PSPI-22, respectively, are serine proteinase inhibitors with different specificity. The 23 kDa protein denoted as PCPI-23 is an inhibitor of plant cysteine proteinases. The PSPI-21 molecule consists of two disulfide-linked polypeptide chains with molecular masses of 16.5 kDa and 4.5 kDa. The PSPI-22 and PCPI-23 have one polypeptide chain. Their amino-termini numbered 212 5 amino acid residues have significant homology to other plant inhibitors which are members of the soybean Kunitz inhibitor family. It is found that at least PSPI-21 and PSPI-22 can predominantly accumulate in potato tubers infected with Phytophthora infestans zoospores.z 1998 Federation of European Biochemical Societies.

A protein of 22 kDa designated as PKTI-22 was isolated from potato tubers (Solanum tuberosum L., cv. Istrinskii) and purified to homogeneity using CM-Sepharose CL-6B ion-exchange chromatography. The protein efficiently suppressed the activity of trypsin, affected chymotrypsin less, and did not affect subtilisin Carlsberg. The N-terminal sequence of PKTI-22 (20 amino acid residues) was found to be highly homologous with the amino acid sequences of the potato Kunitz-type proteinase inhibitors of group B (PKPI-B) that were aligned from the corresponding gene sequences and was identical to the sequence (from the 2nd to the 20th residue) of the recombinant protein PKPI-B10. These data together with the observed similarity of the properties of two proteins indicate that the PKTI-22 protein is encoded by the PKPI-B10 gene.

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