Abstract
Fluorescence lifetime and steady-state fluorescence measurements are used to characterize various mercury/protein and mercury/protein/EDTA complexes. The proteins studied are ovalbumin, α-chymotrypsinogen, and acid phosphatase. Mercury quenches fluorescence in ovalbumin with a change in lifetime, while in α-chymotrypsinogen quenching occurs without a change in lifetime. No quenching by mercury is observed for acid phosphatase. EDTA causes a further small decrease in fluorescence for both mercury/ovalbumin and mercury / α-chymotrypsinogen, while no change is observed for mercury/acid phosphatase. In all cases the decrease in fluorescence intensity is consistent with a static quenching mechanism. The results reported are correlated to previous studies by bromine-81 magnetic resonance spectroscopy.
PDF Article
More Like This
Cited By
You do not have subscription access to this journal. Cited by links are available to subscribers only. You may subscribe either as an Optica member, or as an authorized user of your institution.
Contact your librarian or system administrator
or
Login to access Optica Member Subscription