Carles C
J Dairy Res. 1986 Feb;53(1):35-41. doi: 10.1017/s0022029900024638.
Samples of reduced whole casein from genetically typed individual cows were quantitatively separated into their main components, alpha s1-, alpha s2-, beta- and kappa-caseins by reverse phase high performance liquid chromatography (RP-HPLC) using a mobile phase of phosphate-buffered aqueous propan-2-ol containing sodium dodecyl sulphate and an octadecylsilyl stationary phase. One casein sample was found to give two peaks of beta-casein of approximately equal areas. RP-HPLC of tryptic digests of the two separated peak fractions gave identical patterns with the exception of one peptide peak with different retention times. Amino acid analyses performed on both fractions showed that they corresponded to peptide 114-169 of beta-casein A1. The atypical beta-casein differed from the typical one by a Pro----Leu substitution in region 114-169.
通过反相高效液相色谱法（RP-HPLC），使用含有十二烷基硫酸钠的磷酸盐缓冲丙-2-醇水溶液作为流动相和十八烷基硅烷固定相，对来自基因分型个体奶牛的还原全酪蛋白样品进行定量分离，得到其主要成分αs1-、αs2-、β-和κ-酪蛋白。发现一个酪蛋白样品给出了两个面积大致相等的β-酪蛋白峰。对两个分离的峰级分进行胰蛋白酶消化后的RP-HPLC分析，除了一个肽峰的保留时间不同外，得到了相同的图谱。对两个级分进行的氨基酸分析表明，它们对应于β-酪蛋白A1的114-169肽段。非典型β-酪蛋白与典型β-酪蛋白的区别在于114-169区域的脯氨酸被亮氨酸取代。
