Era S, Kuwata K, Kida K, Sogami M, Yoshida A
Int J Pept Protein Res. 1985 Dec;26(6):575-83. doi: 10.1111/j.1399-3011.1985.tb03214.x.
The acid-induced isomerization (the N-F transition) and expansion of bovine plasma albumin--1-anilino-8-naphthalenesulfonate complex, BPA-ANS1.0 complex (molar ratio of added ANS to BPA = 1.0) were studied by measuring fluorescence and induced CD spectra of ANS. Decrease in the reciprocal of fluorescence polarization, increase in fluorescence intensity and blue shift of fluorescence of ANS in BPA-ANS1.0 complex were correlated with the initial part of the N-F transition and/or the N-F1 transition. Induced CD spectra of ANS showed positive bands at 250-258 and 320-350 nm and one negative band at 280 nm. Most of changes (decreases) in -[theta]280 were also correlated with the initial part of the N-F transition and/or the N-F1 transition. Changes in fluorescence parameters and induced CD spectra of ANS (-[theta]280) might indicate the conformational changes around a strong ANS binding site in the N-terminal domain (Reed et al. (1975), Jonas & Weber (1970) and Brown & Shockley (1982].
