FT-IR study of the Ca2+-binding to bovine alpha-lactalbumin. Relationships between the type of coordination and characteristics of the bands due to the Asp COO- groups in the Ca2+-binding site.
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 Ca2+-binding site of bovine alpha-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 alpha-lactalbumin and EDTA which is the model compound for the pseudo bridging state.
Mizuguchi
M
M
Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo, Japan.
Nara
M
M
Kawano
K
K
Nitta
K
K
D000818:Animals; D001224:Aspartic Acid / Q000378:metabolism*; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism*; D002417:Cattle; D004492:Edetic Acid / Q000378:metabolism; D007768:Lactalbumin / Q000737:chemistry* / Q000378:metabolism*; D017550:Spectroscopy, Fourier Transform Infrared; D013329:Structure-Activity Relationship
D001224:Aspartic Acid; D007768:Lactalbumin; D004492:Edetic Acid; D002118:Calcium