Trujillo A J, Casals I, Guamis B
Tecnologia del Aliments, Centre de Referència en Tecnologia dels Aliments, Facultat de Veterinària, Universitat Autònoma de Barcelona, Bellaterra, Catalonia, Spain.
J Chromatogr A. 2000 Feb 18;870(1-2):371-80. doi: 10.1016/s0021-9673(99)01097-3.
Ovine milk proteins were analyzed both by coupling HPLC and electrospray ionization mass spectrometry (ESI-MS) and by flow injection analysis and ESI-MS detection after separation and collection of fractions from gel permeation chromatography. These methods resolved the four ovine caseins and whey proteins and made it possible to study the complexity of these proteins associated with genetic polymorphism, post-translational changes (phosphorylation and glycosylation) and the presence of multiple forms of proteins. The experimental molecular masses of ewe milk proteins were: 19,373 for kappa-casein 3P; 25,616 for alpha(s2)-casein 10P; 23,411 for alpha(s1)-casein C-8P; 23,750 for beta-casein 5P; 18,170 and 18,148 for beta-lactoglobulins A and B; 14,152 for alpha-lactalbumin A and 66,322 for serum albumin.
通过将高效液相色谱(HPLC)与电喷雾电离质谱(ESI-MS)联用,以及在凝胶渗透色谱分离和收集组分后进行流动注射分析和ESI-MS检测,对羊奶蛋白进行了分析。这些方法解析了四种羊酪蛋白和乳清蛋白,并使得研究与遗传多态性、翻译后修饰(磷酸化和糖基化)以及多种蛋白质形式的存在相关的这些蛋白质的复杂性成为可能。母羊乳蛋白的实验分子量分别为:κ-酪蛋白3P为19,373;α(s2)-酪蛋白10P为25,616;α(s1)-酪蛋白C-8P为23,411;β-酪蛋白5P为23,750;β-乳球蛋白A和B分别为18,170和18,148;α-乳白蛋白A为14,152,血清白蛋白为66,322。