Innocuous character of [ethylenebis(oxyethylenenitrilo)]tetraacetic acid and EDTA as metal-ion buffers in studying Ca2+ binding by alpha-lactalbumin.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference33 articles.
1. Evolution of alpha-lactalbumins. The complete amino acid sequence of the alpha-lactalbumin from a marsupial (Macropus rufogriseus) and corrections to regions of sequence in bovine and goat alpha-lactalbumins.
2. Computation of structures of homologous proteins. .alpha.-Lactalbumin from lysozyme
3. α-Lactalbumin: A calcium metalloprotein
4. Metal ion activation of galactosyltransferase.
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1. Sequential four-state folding/unfolding of goat α-lactalbumin and its N-terminal variants;Proteins: Structure, Function, and Bioinformatics;2012-06-18
2. Thermostable Proteins;Encyclopedia of Industrial Biotechnology;2009-12-15
3. Effect of hydrostatic pressure on unfolding of α-lactalbumin: Volumetric equivalence of the molten globule and unfolded state;Protein Science;2008-12-31
4. Removal of contaminating calcium from buffer solutions used in calcium binding assays;Analytical Biochemistry;2007-06
5. Ca2+ and Na+ binding to high affinity sites of calcium-containing proteins measured by capillary electrophoresis;Journal of Inorganic Biochemistry;2003-06
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