Künkel W, Müller H, May R
Z Allg Mikrobiol. 1975;15(7):523-36.
A purified fraction of crystals stabilized with Cd2+ is prepared from Saccharomyces carlsbergensis protoplasts by means of differential centrifugation. As proved by negative staining the crystals are hexagonal with well preserved surface which in its turn also reveals a hexagonal fine structure. Crystals are digestible by pronase (1 mg/m) in phosphate buffer (pH 7.4). The molecular weight of protein subunits is 38000+/-300D. Amino acid composition of the crude crystal protein is similar to that of microtubular protein (MTP) from brain and sperm, except that lysin content is much higher. The crystal protein exhibits more differences, however, after purification by preparative gel electrophoresis. The level of glycine, alamine, and valine is increased, whereas that of glutamic acid is decreased.
通过差速离心法从卡尔斯伯酵母原生质体中制备用Cd2+稳定的纯化晶体组分。经负染色证明，晶体为六边形，表面保存完好，其表面又呈现出六边形精细结构。晶体可被磷酸盐缓冲液（pH 7.4）中的链霉蛋白酶（1 mg/m）消化。蛋白质亚基的分子量为38000±300D。粗晶体蛋白的氨基酸组成与脑和精子中的微管蛋白（MTP）相似，只是赖氨酸含量高得多。然而，经制备性凝胶电泳纯化后，晶体蛋白表现出更多差异。甘氨酸、丙氨酸和缬氨酸的水平升高，而谷氨酸的水平降低。
