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Fluorescence anisotropy decay studies upon hemoglobin A and its subunits
Author(s) -
Bucci E.,
Fronticelli C.,
Flanigan K.,
Perlman J.,
Steiner R. F.
Publication year - 1979
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1979.360180516
Subject(s) - chemistry , fluorescence , fluorescence anisotropy , anisotropy , hemoglobin , heme , molecule , rotational correlation time , conjugated system , photochemistry , derivative (finance) , biophysics , nuclear magnetic resonance , analytical chemistry (journal) , chromatography , organic chemistry , biochemistry , optics , physics , membrane , financial economics , economics , biology , enzyme , polymer
Abstract Fluorescent conjugates of hemoglobin A, its isolated β‐chain, and the apo‐derivative of the β‐chain have been prepared in which the β‐93 sulfhydryl was conjugated with 1,5‐AEDANS. Radiationless enery transfer to the heme group results in a major decrease in fluorescence intensity and decay time. Measurements of the time decay of fluorescence anisotropy, employing single‐photon counting, indicate that the apparent rotational correlation time is, in each case, substantially reduced from the value expected for a rigid molecule of the same molecular weight. This observation raises the possibility that internal degrees of rotational freedom exist.