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• W2022149843 abstract "Human polymorphonuclear neutrophil (PMN) granule extract (25 m̈g of protein) released 60% of the available 35SO4 from labeled rabbit articular cartilage in 0.5 hour at neutral pH. N-acetyl-L-alanyl-L-alanyl-L-prolyl-L-alanine chloromethyl ketone (NAc-AAPACK), a specific elastase inhibitor, was only minimally effective against whole granule extract, and N-α-tosyl-L-lysine chloromethyl ketone, which inhibits trypsin but not elastase, was completely ineffective. Preparative disc-gel electrophoresis of PMN granule extract revealed two separate regions with independent activity against 35SO4-labeled cartilage. One region contained elastases and, when tested alone, was completely inhibited by NAcAAPACK. The other contained lysozyme and two esterases active against N-acetyl-L-phenylalanine-α-naphthol. Purified lysozyme proved inactive, suggesting that the chymotrypsin-like esterases were responsible for proteoglycan degradation by this region of the gel." @default.
• W2022149843 created "2016-06-24" @default.
• W2022149843 creator A5037419784 @default.
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• W2022149843 date "1975-07-01" @default.
• W2022149843 modified "2023-09-27" @default.
• W2022149843 title "Identification of neutral proteases in human neutrophil granules that degrade articular cartilage proteoglycan" @default.
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• W2022149843 doi "https://doi.org/10.1002/art.1780180413" @default.
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