@article{6381cc03be074b08a50e845b0e409621,
title = "FT-XR study of the Ca2+-binding to bovine α-lactalbumin. Relationships between the type of coordination and characteristics of the bands due to the Asp COO- groups in the Ca2+-binding site",
abstract = "Fourier-tansform 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 Ca2-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 Ca2+ 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.",
keywords = "Ca-binding protein, Coordination type, FT-IR spectroscopy, α-Lactalbumin",
author = "Mineyuki Mizuguchi and Masayuki Nara and Keiichi Kawano and Katsutoshi Nitta",
note = "Funding Information: The COO − antisymmetric stretching vibrations of the glutamyl side-chain give rise to a band at 1567 cm −1 in D 2 O solutions [4] . In the second derivative and Fourier-self deconvolved spectra for the Ca 2+ -bound pike parvalbumin, a strong band found at 1553 cm −1 reflects the bidentate coordinations of the COO − groups of Glu residues in the Ca 2+ -binding sites [5] . This assignment is supported by the X-ray analysis of the Ca 2+ -bound form of pike parvalbumin. The band due to the COO − antisymmetric stretching vibration shifts from 1567 cm −1 to 1553 cm −1 as a result of the coordination of the COO − groups of Glu residues to calcium ions in the bidentate mode. ",
year = "1997",
month = nov,
day = "3",
doi = "10.1016/S0014-5793(97)01274-X",
language = "英語",
volume = "417",
pages = "153--156",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "John Wiley and Sons Inc.",
number = "1",
}