Enami J, Nandi S
Cell Differ. 1977 Oct;6(3-4):217-27. doi: 10.1016/0045-6039(77)90017-3.
SDS-urea polyacrylamide gel electrophoresis of mouse milk proteins revealed the presence of three major phosphoproteins (caseins) of m.w. 44,000, 26,000 and 22,000 daltons. By using an antiserum against crude casein fraction, an immunoprecipitation method was developed for the quantitative measurement of the rate of milk protein synthesis in the mouse mammary tissue. Cultivation of mammary explants with insulin, cortisol and prolactin resulted in the induction of milk protein synthesis as evidenced by the incorporation of [3H]amino acid and [32P]orthophosphate into immune precipitable materials. The present immunoprecipitation method coupled with a simplified explant culture technique provides a suitable procedure for the study of mouse mammary gland differentiation.
对小鼠乳蛋白进行的十二烷基硫酸钠-尿素聚丙烯酰胺凝胶电泳显示，存在分子量分别为44,000、26,000和22,000道尔顿的三种主要磷蛋白（酪蛋白）。通过使用针对粗酪蛋白组分的抗血清，开发了一种免疫沉淀方法，用于定量测定小鼠乳腺组织中乳蛋白的合成速率。用胰岛素、皮质醇和催乳素培养乳腺外植体，导致乳蛋白合成的诱导，这可通过将[3H]氨基酸和[32P]正磷酸盐掺入免疫沉淀物质中得到证明。目前的免疫沉淀方法与简化的外植体培养技术相结合，为研究小鼠乳腺分化提供了一个合适的程序。
