Protein trypsin inhibitor from potato tubers |
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Authors: | T A Revina G V Kladnitskaya N G Gerasimova E L Gvozdeva T A Valueva |
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Institution: | 1.Bach Institute of Biochemistry,Russian Academy of Sciences,Moscow,Russia |
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Abstract: | 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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