Calcium regulates folding and disulfide-bond formation in α-lactalbumin
- 1 September 1989
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 163 (3) , 1390-1396
- https://doi.org/10.1016/0006-291x(89)91133-9
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- α-Lactalbumin: A calcium metalloproteinPublished by Elsevier ,2004
- Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig .alpha.-lactalbuminBiochemistry, 1989
- Crystallographic analysis of the three-dimensional structure of baboon α-lactalbumin at low resolution. Homology with lysozymeBiochemical Journal, 1987
- Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of .alpha.-lactalbumin and lysozymeBiochemistry, 1986
- α-Lactalbumin possesses a novel calcium binding loopNature, 1986
- Physiological roles of zinc and calcium binding to .alpha.-lactalbumin in lactose biosynthesisBiochemistry, 1985
- Formation and isomerization of disulfide bonds in proteins: Protein disulfide-isomerasePublished by Elsevier ,1984
- Role of the environment in the refolding of reduced pancreatic trypsin inhibitorJournal of Molecular Biology, 1980
- Some Kinetic Properties of Human-Milk Galactosyl TransferaseEuropean Journal of Biochemistry, 1974
- Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozymeBiochemistry, 1970