Chianese L, Mauriello R, Intorcia N, Moio L, Addeo F
Istituto di Industrie Agrarie, Università di Napoli Federico II, Portici, Italia.
J Dairy Res. 1992 Aug;59(3):299-305. doi: 10.1017/s0022029900030570.
A new alpha s2-casein variant was isolated from goat milk by means of covalent chromatography. With gel electrophoresis at alkaline pH, the alpha s2-casein variant showed a double band with the highest anodic mobility amongst the casein components. The mobility of the isolated alpha s2-casein variant was similar to that occurring in three individual samples of whole casein. Two dimensional electrophoresis revealed a more pronounced heterogeneity of this protein. Developing the two dimensional plate with polyclonal antibodies obtained against the four main bovine casein fractions, we demonstrated that the variant in question belongs to the alpha s2-casein family. Since the alpha s2-casein fractions, immunospecifically developed, spread along two different zones on the gel, it was concluded that a heterozygous alpha s2-casein form was present in the sample.
通过共价色谱法从山羊奶中分离出一种新的αs2-酪蛋白变体。在碱性pH条件下进行凝胶电泳时，该αs2-酪蛋白变体在酪蛋白组分中显示出阳极迁移率最高的双条带。分离出的αs2-酪蛋白变体的迁移率与全酪蛋白的三个单独样品中出现的迁移率相似。二维电泳显示该蛋白质具有更明显的异质性。用针对四种主要牛酪蛋白组分获得的多克隆抗体对二维平板进行显影，我们证明所讨论的变体属于αs2-酪蛋白家族。由于免疫特异性显影的αs2-酪蛋白组分在凝胶上沿两个不同区域分布，因此得出结论，样品中存在杂合的αs2-酪蛋白形式。
