An experimental artifact in the use of chelating metal ion buffers. Binding of chelators to bovine alpha-lactalbumin.
Open Access
- 1 May 1983
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 258 (9) , 5707-5709
- https://doi.org/10.1016/s0021-9258(20)81950-4
Abstract
No abstract availableThis publication has 9 references indexed in Scilit:
- α-Lactalbumin: A calcium metalloproteinPublished by Elsevier ,2004
- Metal ion binding to .alpha.-lactalbumin speciesBiochemistry, 1982
- Characteristics of the binding of Ca2+ and other divalent metal ions to bovine alpha-lactalbumin.Journal of Biological Chemistry, 1981
- Calcium binding to α-lactalbumin: Structural rearrangement and association constant evaluation by means of intrinsic protein fluorescence changesBiochemical and Biophysical Research Communications, 1981
- The pH dependence of tryptophan fluorescence of goat α-lactalbumin with particular reference to the effect of binding of an impurity from milkBiochimica et Biophysica Acta (BBA) - Protein Structure, 1980
- Comparative fluorescence properties of bovine, goat, human and guinea pig α lactalbuminBiophysical Chemistry, 1980
- [15] Studies of protein ligand binding by gel permeation techniquesPublished by Elsevier ,1973
- The dependence of contraction and relaxation of muscle fibres from the crab Maia squinado on the internal concentration of free calcium ionsBiochimica et Biophysica Acta (BBA) - Specialized Section on Biophysical Subjects, 1964
- Improved method for the preparation of crystalline β-lactoglobulin and α-lactalbumin from cow's milkBiochemical Journal, 1957