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Changes in the fluoresence of N-acetyl-N'-(5-sulfo-l-naphthyl)ethylenediamine (EDANS), being attached to Cys-674 of sarcoplasmic reticulum Ca2+-ATPase without affecting the catalytic activity, as well as changes in the intrinsic tryptophan fluorescence were followed throughout the catalytic cycle by the steady-state measurements and the stopped-flow spectrofluorometry. EDANS-fluorescence changes reflect conformational changes near the ATP binding site in the cytoplasmic domain, while mostdoi:10.1007/bf01788364 pmid:8825034 fatcat:dt4mmk4kmbgrlhkihrnty7g5cm