Purification and structure of novel cysteine proteinase inhibitors, staccopins P1 and P2, from Staphylococcus tanabeensis.
- 1 January 1987
- journal article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 51 (3) , 861-868
- https://doi.org/10.1271/bbb1961.51.861
Abstract
A new type of cysteine proteinase inhibitors, staccopin P1 and P2, are low molecular weight (lower than 1, 000) peptide derivatives isolated first from Staphylococcus sp. Staccopins strongly inhibited only cysteine proteinases like calpain and papain, but were not active against serine proteinases like trypsin and chymotrypsin. The purification procedures included HP-20 adsorption chromatography, DEAE-cellulose, CM-cellulose, Sephadex LH-20 column chromatography, and high-performance liquid chromatography. The yields were 49 mg and 18mg from 20 liters each of culture fluid. These proteinase inhibitors are pentapeptides containing valine and phenylalaninal for staccopin P1 or tyrosinal for staccopin P2, and the N-terminals of both pep tides are free. Thus the structures are H-valyl-valyl-valyl-valyl-phenylalaninal for staccopin P1 and H-valyl-valyl-valylvalyl-tyrosinal for staccopin P2. The amino acid sequence-inhibitory activity relationships of Staccopins and other low molecular weight peptide cysteine proteinase inhibitors derived from natural sources are discussed.Keywords
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