Giannitsis D J
Arzneimittelforschung. 1978;28(11):2158-9.
Histone fractions from human leukocyte nuclei can interact with heparin to form complexes measurable by means of laser nephelometry. Histone fractions have not all the same affinity to bound heparin and the lysinrich histone fraction cannot interact with heparin. The formation of histone/heparin complex depends not on the temperature between 20 degrees--37 degrees C or on the pH between 7--8.2. The precision of the method was estimated. The significance of the histones/heparin interactions for an assay method for control to the biological activity of heparin preparations and a possible biological role of these interactions in vivo was briefly discussed.
来自人白细胞细胞核的组蛋白组分可与肝素相互作用,形成能用激光散射比浊法测定的复合物。并非所有组蛋白组分对结合的肝素都有相同的亲和力,富含赖氨酸的组蛋白组分不能与肝素相互作用。组蛋白/肝素复合物的形成不取决于20摄氏度至37摄氏度之间的温度,也不取决于7至8.2之间的pH值。评估了该方法的精密度。简要讨论了组蛋白/肝素相互作用对于肝素制剂生物活性控制测定方法的意义以及这些相互作用在体内可能的生物学作用。