Premium
FT‐IR study of the Ca 2+ ‐binding to bovine α‐lactalbumin
Author(s) -
Mizuguchi Mineyuki,
Nara Masayuki,
Kawano Keiichi,
Nitta Katsutoshi
Publication year - 1997
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/s0014-5793(97)01274-x
Subject(s) - chemistry , crystallography , infrared spectroscopy , antisymmetric relation , lactalbumin , spectroscopy , fourier transform infrared spectroscopy , binding site , stereochemistry , biochemistry , organic chemistry , physics , quantum mechanics , mathematical physics
Fourier‐transform infrared spectroscopy (FT‐IR) was applied to examine relationships between the type of coordination and the COO − antisymmetric and symmetric stretches of the COO − groups in the Ca 2+ ‐binding site of bovine α‐lactalbumin. The peaks at 1593, 1578, 1425, and 1403 cm −1 were assigned to the COO − groups of Asp‐82, 87, and 88 coordinating to Ca 2+ in the pseudo bridging mode, according to the results of X‐ray crystallography. The bands due to the COO − groups were quite similar to each other between α‐lactalbumin and EDTA which is the model compound for the pseudo bridging state.