Release of alkaline phosphatase from membranes by a phosphatidylinositol-specific phospholipase C.
نویسندگان
چکیده
Purified phosphatidylinositol-specific phospholipase C from Staphylococcus aureus released a substantial proportion of the total alkaline phosphatase activity from a wide range of tissues from several mammalian species. Co-purification of the phospholipase C and alkaline phosphatase-releasing activities and the inhibition of both these activities by iso-osmotic salt solutions suggested that the releasing effect was unlikely to be due to a contaminant.
منابع مشابه
Enzymes linked to phosphatidylinositol in plasma membranes.
Treatment of tissues, isolated cells, and cell homogenates and fractions with a phosphatidylinositol-specific phospholipase C has demonstrated a selective release of several enzymes from plasma membranes. The purified phospholipase has no detectable action on mammalian phospholipids other than phosphatidylinositol and although this phospholipid appears to form only a very small proportion of th...
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Alkaline phosphatase (ALP) is attached to the cell surface in mammalian tissues via a glycosyl-phosphatidylinositol (GPI) anchor and can be released from the membrane by GPI-specific phospholipases. In a range of cultured human cell lines, however, the sensitivity of ALP to phospholipases was observed to be variable in magnitude (approximately 20-90%). The mechanism of phospholipase resistance ...
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ورودعنوان ژورنال:
- The Biochemical journal
دوره 167 1 شماره
صفحات -
تاریخ انتشار 1977