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Evidence for the binding states of copper(II)–serum albumin complexes as revealed by transient electric dichroism measurements
Author(s) -
Yamagishi Akihiko
Publication year - 1981
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.1981.360200114
Subject(s) - chemistry , chromophore , circular dichroism , copper , bovine serum albumin , dichroism , linear dichroism , crystallography , serum albumin , transient (computer programming) , molecule , photochemistry , chromatography , organic chemistry , biochemistry , optics , physics , computer science , operating system
Transient electric dichroism has been measured for a Cu(II)–bovine serum albumin (BSA)–2‐(2‐pyridylazo)‐1‐naphthol (αPAN) complex at pH 5.5–12. From the magnitude of the reduced linear dichroism and the disorientation rate of the oriented chromophore, at least three kinds of binding states of Cu(αPAN) + complex exist. They are present predominantly at pH 5.5–10, 7.5–10, and 10–12, with the αPAN plane approximately parallel, vertical, and parallel with respect to the oriented axis of a BSA molecule.