Lampreave F, Piñeiro A, Brock J H, Castillo H, Sánchez L, Calvo M
Departmento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad de Zaragoza, Spain.
Int J Biol Macromol. 1990 Feb;12(1):2-5. doi: 10.1016/0141-8130(90)90073-j.
The association between bovine lactoferrin and the major bovine whey proteins, beta-lactoglobulin, alpha-lactalbumin and albumin has been studied by immunochemical techniques, gel filtration and affinity chromatography in lacteal secretions and using purified proteins. Bovine lactoferrin is able to form non-covalent complexes with beta-lactoglobulin or albumin, with lactoferrin-protein molar ratios of 2:1 and 1:1 respectively. No association was detected with alpha-lactalbumin. Lactoferrin interacts with beta-lactoglobulin-Sepharose at low ionic strength, but not in the presence of 0.3 M NaCl, indicating that ionic interactions are important. The lack of association with alpha-lactalbumin suggests however a certain degree of specificity in this electrostatic interaction.
通过免疫化学技术、凝胶过滤和亲和色谱法，在乳状分泌物中并使用纯化蛋白，研究了牛乳铁蛋白与主要的牛乳清蛋白（β-乳球蛋白、α-乳白蛋白和白蛋白）之间的关联。牛乳铁蛋白能够与β-乳球蛋白或白蛋白形成非共价复合物，乳铁蛋白与蛋白质的摩尔比分别为2:1和1:1。未检测到与α-乳白蛋白有结合。乳铁蛋白在低离子强度下与β-乳球蛋白-琼脂糖相互作用，但在0.3M NaCl存在时则不相互作用，这表明离子相互作用很重要。然而，与α-乳白蛋白缺乏结合表明这种静电相互作用存在一定程度的特异性。
