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Suitability and appropriateness of fluorescence correlation spectroscopy (FCS) to biological and chemical studies are discussed with reference to its sensitivity, spatial and temporal resolution. Data indicate that FCS is an excellent tool to molecular structure, chemical kinetics, single-cell reactions, and lipid diffusion in membranes.

A study was conducted to determine conditions that allow the selective alteration of an ATP-protectable site on the Ca-ATPase in skeletal sarcoplasmic reticulum membranes by erythrosin isothiocyanate. An ammonium molybdate complex of phosphate was utilized to measure calcium-dependent ATPase activity while mass spectra was determined by an Autospec-Q tandem hybrid mass spectrometer. Results showed that erythrosin isothiocyanate interacts with either ATP binding or the structural coupling between a low-affinity ATP-binding site and the phosphoanhydride at Asp(sub 351).