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- W2002143946 abstract "1. Using low salt, Triton X-100 and high salt extracts of bovine atria, two main proteinases were identified by means of fluorogenic oligopeptide substrates. 2. An acidic proteinase, extracted in low salt and Triton X-100 was identified as cathepsin B, but it caused little hydrolysis of the Z-Gly-Pro-Arg- containing substrate that resembles the cleavage site for activation of pro-ANF. 3. An alkaline proteinase was extracted only with high salt and had characteristics of the serine proteinase tryptase. It cleaved Z-Gly-Pro-Arg- containing substrates more efficiently than others tested and was localized in and around mast cells histochemically. Previously, Imada et al., 1988 (J. biol. Chem. 263, 9515-9519) found an identical enzyme would cleave ANF from pro-ANF. 4. These results suggest therefore that mast cell tryptase may be involved in the activation of ANF from pro-ANF." @default.
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- W2002143946 date "1991-01-01" @default.
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- W2002143946 title "Proteinase activities in bovine atrium and the possible role of mast cell tryptase in the processing of Atrial Natriuretic Factor (ANF)" @default.
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- W2002143946 doi "https://doi.org/10.1016/0305-0491(91)90151-3" @default.
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