The Method of Aschaffenburg and Drewry for the Crystallization of β-Lactoglobulin and α-Lactalbumin. 1. Electrophoresis of Fractions and the Calcium2+/Ethylenebis (Oxyethylenenitrilo) Tetraacetic Acid Shift of α-Lactalbumin
Author:
Publisher
American Dairy Science Association
Subject
Genetics,Animal Science and Zoology,Food Science
Reference23 articles.
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2. Crystallography of α-lactalbumin III. Crystals of baboon milk α-lactalbumin;Aschaffenburg;J. Mol. Biol.,1979
3. Manganese (II) electron spin resonance and cadmium-113 nuclear magnetic resonance evidence for the nature of the calcium binding site in α-lactalbumins;Berliner;Biochemistry,1983
4. The isolation and identification of the B protein of lactose synthetase as α-lactalbumin;Brodbeck;J. Biol. Chem.,1967
5. Cyclic 3′,5′-nucleotide phosphodiesterase from bovine heart;Butcher,1974
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1. References;Structure–Function Properties of Food Proteins;1994
2. Identification of human milk α-lactalbumin as a cell growth inhibitor;Protoplasma;1992-12
3. Chromatographic and electrophoretic methods used for analysis of milk proteins;Journal of Chromatography A;1992-10
4. Isolation of β-Lactogobulin and α-Lactalbumin by Gel Filtration Using Sephacryl S-200 and Purification by Diethylaminoethyl Ion-Exchange Chromatography;Journal of Dairy Science;1990-09
5. Phylogenetic Variations in the Calcium-Dependent Electrophoretic Shift of α-Lactalbumin;Journal of Dairy Science;1989-12
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