Primary structure of cathepsin D inhibitor from potatoes and its structure relationship to soybean trypsin inhibitor family
Language English Country England, Great Britain Media print
Document type Comparative Study, Journal Article
PubMed
2753167
DOI
10.1016/0014-5793(89)81435-8
PII: 0014-5793(89)81435-8
Knihovny.cz E-resources
- MeSH
- Protease Inhibitors * isolation & purification MeSH
- Trypsin Inhibitors * MeSH
- Cathepsin D antagonists & inhibitors MeSH
- Trypsin Inhibitor, Kunitz Soybean * MeSH
- Molecular Sequence Data MeSH
- Proteins * isolation & purification MeSH
- Plant Proteins * MeSH
- Amino Acid Sequence MeSH
- Solanum tuberosum enzymology MeSH
- Publication type
- Journal Article MeSH
- Comparative Study MeSH
- Names of Substances
- CDI protein, Solanum tuberosum MeSH Browser
- Protease Inhibitors * MeSH
- Trypsin Inhibitors * MeSH
- Cathepsin D MeSH
- Trypsin Inhibitor, Kunitz Soybean * MeSH
- Proteins * MeSH
- Plant Proteins * MeSH
A novel effective procedure for the purification of cathepsin D inhibitor from potatoes (PDI) was developed. The amino acid sequence of PDI was determined by analysis of the cyanogen bromide digest and of the limited tryptic and chymotryptic digest of the protein. The inhibitor is a single polypeptide chain protein consisting of 188 residues with a simple sugar moiety attached to Asn-19. The tentative disulfide pairings are also suggested. The sequence data clearly indicate that PDI is homologous with the soybean trypsin inhibitor (STI) (Kunitz) family. The active center of PDI for trypsin inhibition was identified as Pro-Val-Arg-Phe in analogy to STI.
References provided by Crossref.org
Characterization of gut-associated cathepsin D hemoglobinase from tick Ixodes ricinus (IrCD1)
