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- W1999906672 abstract "A new type of cysteine proteinase inhibitors, staccopin PI 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 18 mg from 20 liters each of culture fluid. These proteinase inhibitors are pentapeptides containing valine and phenylalaninal for staccopin PI or tyrosinal for staccopin P2, and the N-terminals of both peptides are free. Thus the structures are H-valyl-valyl-valyl-valyl-phenylalaninal for staccopin PI and H-valyl-valyl-valyl- valyl-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." @default.
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- W1999906672 date "1987-03-01" @default.
- W1999906672 modified "2023-10-16" @default.
- W1999906672 title "Purification and Structure of Novel Cysteine Proteinase Inhibitors, Staccopins P1 and P2, from Staphylococcus tanabeensis" @default.
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- W1999906672 doi "https://doi.org/10.1080/00021369.1987.10868093" @default.
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