Inactivation of sarcoplasmic reticulum (Ca + Mg)-ATPase by N-cyclohexyl-N′-(4-dimethylamino-α-naphthyl)carbodiimide |
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Authors: | C.C. Chadwick E.W. Thomas |
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Abstract: | The synthesis and characterisation of N-cyclohexyl-N′-(4-dimethylamino-α-naphthyl)carbodiimide (NCD-4) is described. Only the N-acetylurea and urea corresponding to NCD-4 are appreciably fluorescent: the O-phenylisourea and S-ethylisothiourea derivatives have negligible fluorescence. NCD-4 inhibits the (Ca2+ + Mg2+)-ATPase of sarcoplasmic reticulum irreversibly: Ca2+ protects against inhibition. Covalent incorporation of NCD-4 occurs into the Ca2+-protected sites, with a stoichiometry of approximately 1 mole/mole of ATPase. The modified enzyme has fluorescence emission properties similar to those of NCD-4 N-acetylurea in a relatively hydrophobic environment: it is concluded that NCD-4 has modified a carboxylate group (s) located in or near the Ca2+-binding sites of the ATPase. |
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Keywords: | (Ca2+ + Mg2+)-ATPase inactivation Fluorescent label Cyclohexyl(dimethylaminonaphthyl)carbodiimide (Sarcoplasmic reticulum) |
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