Henkin R I, Lippoldt R E, Bilstad J, Wolf R O, Lum C K, Edelhoch H
J Biol Chem. 1978 Oct 25;253(20):7556-65.
A chromatographic procedure for purification of the proteins in human parotid saliva has been developed. The eluates of a Sephadex G-150 and two ion exchange columns have been analyzed simultaneously by several physical and chemical tests; these include three optical properties of proteins, assays for neutral sugars, sialic acid and zinc, and disc gel electrophoresis. The ratios of the different variables have been used to determine the homogeneity and complexity of the protein distribution in the various peaks of the chromatographic eluates. By chromatographic methods, it has been possible to purify a glycoprotein with unusual staining characteristics and amino acid composition. Glycoproteins with similar properties comprise a major portion of the proteins in parotid saliva and appear to constitute a family of related proteins which differ in molecular size, carbohydrate and sialic acid content, and electrophoretic mobility. The fractionation of several enzymes in parotid saliva is also reported.
已开发出一种用于纯化人腮腺唾液中蛋白质的色谱方法。通过多种物理和化学测试同时分析了葡聚糖凝胶G - 150和两个离子交换柱的洗脱液；这些测试包括蛋白质的三种光学性质、中性糖、唾液酸和锌的测定以及圆盘凝胶电泳。不同变量的比率已用于确定色谱洗脱液各个峰中蛋白质分布的均匀性和复杂性。通过色谱方法，已能够纯化出具有异常染色特性和氨基酸组成的糖蛋白。具有相似性质的糖蛋白占腮腺唾液中蛋白质的主要部分，并且似乎构成了一个相关蛋白质家族，它们在分子大小、碳水化合物和唾液酸含量以及电泳迁移率方面存在差异。还报道了腮腺唾液中几种酶的分离情况。
