| Literature DB >> 20331422 |
T A Revina1, G V Kladnitskaya, N G Gerasimova, E L Gvozdeva, T A Valueva.
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.Entities:
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Year: 2010 PMID: 20331422 DOI: 10.1134/s0006297910010050
Source DB: PubMed Journal: Biochemistry (Mosc) ISSN: 0006-2979 Impact factor: 2.487