Premium
A SPECTROSCOPIC STUDY OF THE HEMIN‐HUMAN‐α‐FETOPROTEIN SYSTEM
Author(s) -
ŽiŽkovský V.,
Havranová M.,
Štrop P.,
Korčáková J.
Publication year - 1983
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1983.tb32848.x
Subject(s) - hemin , chemistry , biochemistry , heme , enzyme
The binding of hemin to human alpha-fetoprotein has been estimated by means of fluorescence and spectrophotometric titration. Spectrophotometric titration discloses one strong binding site for hemin with an association constant of 1.5 X 10(7) M-1. The binding causes a shift of the absorption maximum to a higher wavelength and a rise in the molar absorption coefficient. Fluorescence reveals that the binding of hemin to human AFP quenches the protein fluorescence, which changes in character from a tryptophan type to a tyrosine type. As postulated by our results, the binding of hemin to human AFP is similar to the binding of hemin to HSA.