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- W1969135423 abstract "Two membrane-bound acid phosphatases (B) and (C) were purified and their physicochemical properties compared to those of a cytoplasmic acid phosphatase (A). The preparations were homogeneous by polyacrylamide gel electrophoresis (PAGE). The apparent molecular weights were: 55 000 ± 2000 (enzyme B), 65 000 ± 2000 (enzyme C) and 98 000 ± 2000 (enzyme A). Phosphorylated sugars were hydrolysed only by the membrane-bound acid phosphatases, whereas the cytoplasmic enzyme showed no effect on four of the five phosphorylated sugars studied. The enzymatic activities of all three enzymes were inhibited by Ca2+, Hg2+, Mo, EDTA, but stimulated by several ions, particularly by Mg2+." @default.
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- W1969135423 date "1983-12-01" @default.
- W1969135423 modified "2023-10-14" @default.
- W1969135423 title "Properties of two membrane-bound acid phosphatases compared with those of a cytoplasmic acid phosphatase from Dioscorea cayenensis rotundata" @default.
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- W1969135423 doi "https://doi.org/10.1016/0304-4211(83)90036-6" @default.
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