Premium
Interaction of actin with dansyl‐tropomyosin
Author(s) -
Burtnick L.D.,
Bhangu K.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80426-4
Subject(s) - chemistry , fluorescence , actin , tropomyosin , dansyl chloride , fluorescence anisotropy , biophysics , chloride , cationic polymerization , photochemistry , biochemistry , chromatography , organic chemistry , mass spectrometry , derivatization , biology , physics , quantum mechanics , membrane
5‐[Dimethylamino]naphthalene‐1‐sulfonyl chloride (dansyl chloride) reacts with rabbit skeletal muscle tropomyosin (TM) to yield a highly fluorescent product, DNS‐TM. The extent of modification of TM can be regulated over a wide range, 0.3–15.5 dansyl groups per TM, depending upon the temperature and duration of the reaction. However, under all conditions employed, about 15 different fluorescent tryptic peptides of TM were produced. DNS‐TM undergoes end‐to‐end polymerization at low ionic strengths, but to a somewhat lesser extent than unlabelled TM does. DNS‐TM also binds muscle F‐actin. This interaction may be followed fluorimetrically by observing a blue‐shift in emission maximum, an increase in fluorescence intensity or an increase in fluorescence polarization of the DNS‐TM complex with F‐actin.