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- W2011045082 abstract "Phospholipase A2 activity was detected in a secretory granular fraction (SG) purified by Percoll gradient centrifugation from rat parotid gland using [3H]phosphatidylcholine (PC) as a substrate. High activity of this enzyme was observed at neutral pH. The enzyme was activated by Triton X-100 and did not require Ca2+ for its activity. In the absence of Ca2+, its apparent Km for exogenous PC was 28 μM while it was slightly increased by adding 5 mM CaCl2 (73 μM). Furthermore, the enzyme was located essentially in a granular membrane fraction separated from granular lysate. The deacylation activities were also detected in other subcellular fractions, which showed a different detergent-susceptibility of pH-dependency from that in SG. These results suggest that secretory granules have membrane-bound phospholipase A2 which has properties different from that found in other organelles." @default.
- W2011045082 created "2016-06-24" @default.
- W2011045082 creator A5041110839 @default.
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- W2011045082 date "1991-06-01" @default.
- W2011045082 modified "2023-10-15" @default.
- W2011045082 title "Ca2+-independent phospholipase A2 activity associated with secretory granular membranes in rat parotid gland" @default.
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- W2011045082 doi "https://doi.org/10.1016/0005-2760(91)90050-r" @default.
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