Sobieski R J, Johnson T C, Sharifi B G, Bascom C C
Life Sci. 1986 May 19;38(20):1883-8. doi: 10.1016/0024-3205(86)90144-x.
A bovine sialoglycopeptide, purified to homogeneity and capable of inhibiting cellular protein synthesis and proliferation, was shown to agglutinate a wide variety of nontransformed and transformed cells. The cell agglutination activity was shown to be independent of the biological inhibitory action and most likely related to a protease activity that could not be physically separated during purification of the sialoglycopeptide. Samples that were completely biologically inactivated retained full protease activity and their ability to agglutinate target cells. Balb/c 3T3 cells were not agglutinated by the sialoglycopeptide and they elicited a protein that interfered with the agglutination reaction and even redispursed cells that already had been aggregated by the inhibitor.
一种纯化至同质且能够抑制细胞蛋白质合成与增殖的牛唾液酸糖肽，被证明能凝集多种未转化和已转化的细胞。细胞凝集活性被证明与生物抑制作用无关，且很可能与一种在唾液酸糖肽纯化过程中无法物理分离的蛋白酶活性有关。完全丧失生物活性的样品仍保留全部蛋白酶活性及其凝集靶细胞的能力。Balb/c 3T3细胞不会被该唾液酸糖肽凝集，它们会产生一种蛋白质，这种蛋白质会干扰凝集反应，甚至能使已被该抑制剂凝集的细胞重新分散。
