Kawakami H, Shinmoto H, Dosako S, Sogo Y
J Dairy Sci. 1987 Apr;70(4):752-9. doi: 10.3168/jds.s0022-0302(87)80070-x.
Immunoaffinity columns made with monoclonal antibodies to either human or bovine lactoferrins were prepared to isolate human lactoferrin or bovine lactoferrin from milks by a single chromatographic step. Recoveries of human lactoferrin and bovine lactoferrin were 98 and 97%, respectively. The human lactoferrin recovered from defatted human colostrum was 98% pure with 93% iron-binding capacity. Amount of recovered bovine lactoferrin, as well as purity and iron-binding capacity, varied widely depending on the source of bovine milks and pretreatments (particularly pasteurization temperature). The best source to isolate bovine lactoferrin was raw skim milk yielding a protein 97% pure and with a 99% iron-binding capacity. Thus, immunoaffinity chromatography provides an effective one-pass isolation of highly pure human or bovine lactoferrin with reasonable recovery and iron-binding capacity.
制备了分别针对人乳铁蛋白或牛乳铁蛋白的单克隆抗体免疫亲和柱,用于通过一步色谱法从牛奶中分离人乳铁蛋白或牛乳铁蛋白。人乳铁蛋白和牛乳铁蛋白的回收率分别为98%和97%。从脱脂人初乳中回收的人乳铁蛋白纯度为98%,铁结合能力为93%。回收的牛乳铁蛋白的量以及纯度和铁结合能力因牛乳来源和预处理(特别是巴氏杀菌温度)的不同而有很大差异。分离牛乳铁蛋白的最佳来源是原料脱脂乳,得到的蛋白纯度为97%,铁结合能力为99%。因此,免疫亲和色谱法能有效地一次性分离出高纯度的人或牛乳铁蛋白,回收率和铁结合能力合理。