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- W2006238434 abstract "Lanthanide derivatives of the zinc metalloprotein, phospholipase C (Bacillus cereus), have been formed. Their reactivation from the half-apo enzyme (one zinc atom removed) was found to be very pH-dependent. The maximum reactivation activity obtained between pH 7–8 is approx. 40% of the native protein. Both the native enzyme and the Gd3+-derivative show a plateau in activity toward dimyristoylphosphatidylcholine/Triton X-100 mixed micelles between pH 5.5–8.5 with an acid pKa of 4.6 and a basic pKa of 10.3. Substrate specificity is unchanged by lanthanide substitution: no activity is observed toward sphingomyelin or ether-linked lecithins. Both metalloenzymes show parallel ‘surface dilution’ kinetics towards dimyristoylphosphatidylcholine solubilized in mixed micelles with cetyltrimethylammonium bromide, zwittergent 3–14 and deoxycholate. However, the Gd3+-derivative appears to be more strongly inhibited by Triton X-100 than the native enzyme. This may reflect a decreased Ki for the nonionic detergent. Because of its similarity to the native protein, the Gd3+-derivative is a very useful probe for NMR studies of protein interactions with lipids and detergents. For example, cetyltrimethylammonium bromide, a cationic detergent, binds tightly to the enzyme. The N-methyl protons are preferentially broadened over bulk methylene and the terminal methyl group when the detergent is bound to the protein, indicating the proximity of this part of the molecule to the substituted metal site on phospholipase C." @default.
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- W2006238434 title "Lanthanide derivatives of phospholipase C from Bacillus cereus" @default.
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- W2006238434 doi "https://doi.org/10.1016/0167-4838(83)90202-9" @default.
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