Influence of zinc (II) binding on the structure of bovine α-lactalbumin
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3011.1996.tb01339.x/fullpdf
Reference27 articles.
1. 1H-NMR assignments and local environments of aromatic residues in bovine, human and guinea pig variants of alpha-lactalbumin
2. Refined structure of baboon α-lactalbumin at 1.7 Å resolution
3. Alpha-lactalbumin possesses a distinct zinc binding site.
4. Some Kinetic Properties of Human-Milk Galactosyl Transferase
5. Lactose synthase. An investigation of the interaction site of alpha-lactalbumin for galactosyltransferase by differential kinetic labeling.
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1. Influence of divalent metal cations on α-lactalbumin fibril formation;JBIC Journal of Biological Inorganic Chemistry;2024-08-10
2. Functionalization of Alpha-Lactalbumin by Zinc Ions;ACS Omega;2022-10-21
3. α-Lactalbumin, Amazing Calcium-Binding Protein;Biomolecules;2020-08-20
4. Effects of zinc binding on the structure and thermal stability of camel alpha-lactalbumin;Journal of Thermal Analysis and Calorimetry;2014-11-29
5. The pressure-induced structural change of bovine α-lactalbumin as studied by a fluorescence hydrophobic probe;International Journal of Peptide and Protein Research;2009-01-12
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