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Intrinsic fluorescence of purified calcium pump reconstituted in 1,2-diacylphosphatidylcholines with monounsaturated acyl chains

Elsevier B.V.
Publication Date
  • Biochemistry > Amino Acids And Peptides And Proteins
  • Biochem/0404001
  • Biology


The specific ATP phosphohydrolase activity of purified sarcoplasmic reticulum calcium pump (E.C. reconstituted into 1,2-diacylphosphatidylcholines with monounsaturated acyl chains (diCn:1PC, n = 14-24 is the number of acyl chain carbons) is maximal at the acyl chain length of n=18 carbons and decreases for longer or shorter acyl chains. The intrinsic fluorescence spectra of reconstituted protein dispersed in buffer (0.2 mol/l Hepes, 0.1 mol/l KCl, 0.005 mol/l MgSO 4, 25 μmol/l EGTA, pH7.2) were recorded and fitted with the exponentially modified Gaussian function. The spectral parameters obtained indicate that the tryptophanyl residues responsible for the intrinsic fluorescence of the protein are located in sites which hydrophobicity increases with the diCn:1PC acyl chain length; simultaneously, the heterogeneity of these sites is changed.

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