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- W966875535 abstract "This chapter describes assay, purification, and properties of myeloblastin. Myeloblastin is a neutral serine endopeptidase produced during myeloid differentiation and stored in the azurophilic granules of polymorphonuclear leukocytes (PMNs). Assays for myeloblastin are based on its preference for small aliphatic amino acids at the P1 site of susceptible peptide bonds. Although myeloblastin degrades a wide variety of extracellular matrix molecules, including elastin, fibronectin, vitronectin, collagen type IV, and the core protein of proteoglycans, the esterolytic or amidolytic activity of the enzyme against selected blocked amino acid or oligopeptide substrates has proved to be most useful in assessing enzyme activity. t-butyloxy carbonyl p-nitrophenylester is a nonspecific and sensitive substrate that is suitable to work with myeloblastin particularly in studies evaluating inhibitors. Release of p-nitrophenol is measured by the increase in absorbance at 347.5 nm. Myeloblastin is a basic protein and appears as three isoforms in polyacrylamide gel electrophoresis at neutral pH. It is inhibited by typical inhibitors of serine peptidases, such as phenylmethylsulfonyl fluoride and diisopropyl fluorophosphates." @default.
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- W966875535 date "1994-01-01" @default.
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- W966875535 title "[3] Myeloblastin: Leukocyte proteinase 3" @default.
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- W966875535 doi "https://doi.org/10.1016/0076-6879(94)44005-0" @default.
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