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- W2034257952 abstract "Three forms (I, II and III) of phospholipase C were separated from the cytosol of bovine aorta by chromatography on Blue Sepharose. All three forms showed an increase of enzyme activity when free Ca2+ in the assay was raised between 40 μM and 9 mM. The pH optimum was in the range of 6.0 to 6.5 for each subtype. Marked differences in thermostability were found when the three enzyme forms were pre-incubated at 50°C prior to the assay. All three forms were able to hydrolyse phosphatidylinositol as well as phosphatidylinositol 4-phosphate and phosphatidylnositol 4,5-biophosphate. In contrast, when phosphatidylcholine was used as substrate, no enzyme activity was observed. Spermine and spermide, but bot putrescine, were able to stimulate form I and III; neomycin sulphate inhibited all three subtypes." @default.
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- W2034257952 date "1991-01-01" @default.
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- W2034257952 title "Characterization of multiple forms of phosphoinositide-specific phospholipase C from bovine aorta" @default.
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- W2034257952 doi "https://doi.org/10.1016/0898-6568(91)90059-4" @default.
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