PREPARATION AND PROPERTIES OF HUMAN FIBRINOGEN OF RELATIVELY HIGH SOLUBILITY
PREPARATION AND PROPERTIES OF HUMAN FIBRINOGEN OF RELATIVELY HIGH SOLUBILITY
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DOI：
10.1021/bi00873a008
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发表时间：
1966-01-01
期刊：
影响因子：
2.9
通讯作者：
SHERRY, S
中科院分区：
文献类型：
--
作者：
MOSESSON, MW;SHERRY, S
目前用于分离和纯化人纤维蛋白原的大多数方法都倾向于排除在最终产品制备过程中溶解度相对较高和较低的可溶和不可溶物质（例如Blomback组分1-4）。建立了一种纯化分离高溶解度人纤维蛋白原的方法，采用血浆甘氨酸沉淀法，以2.1[图像]甘氨酸在5[度]下进行初始分离。在甘氨酸再沉淀纤维蛋白原部分，并去除冷不溶性部分（1-1）之后，8 - 16%乙醇浓度的纤维蛋白原（1-5）比在8%乙醇浓度（1-2）下可沉淀的纤维蛋白原（1-5）更易溶解，平均可溶性为91%。用乙醇进一步分离1-5，可以更完全地分离高溶解度纤维蛋白原和低溶解度纤维蛋白原，所得部分被命名为di -7，具有约95%的吸附性。甘氨酸对1-7的再沉淀远没有预期的完整，但得到的材料始终保持97%或更高的可穿戴性。这种观察到的甘氨酸沉淀性的变化可归因于它与溶解度较低的纤维蛋白原的相对分离，它似乎与纤维蛋白原相互作用。分离纤维蛋白原减法（1-3至1-8）的溶解度研究清楚地表明了这些组分之间的差异，尽管所有组分都是异质的。各种减水剂对凝血酶的生物反应性与其溶解度直接相关；溶解度越高，凝血酶时间越长。
Most of the methods now employed for the isolating and purification of human fibrinogen tend to exclude material, both clottable and nonclottable, of relatively higher and lower solubility during the preparation of the final product (e.g. Blomback fraction 1-4). A method for the purification and isolation of human fibrinogen of high solubility was developed which employed glycine precipitation of plasma with 2.1 [image] glycine at 5[degree] for the initial isolation. Subsequent to glycine reprecipitatlon of the fibrinogen fraction, and removal of a cold-Insoluble fraction (1-1), fractionatlon between 8 and 16% ethanol concentration yielded fibrinogen (1-5) which was more soluble than the fibrinogen preciptable at 8% ethanol concentration (1-2) and which averaged 91% clottable. Further subfractlonation of 1-5 with ethanol served to isolate more completely the high solubility, fibrinogen from that of lower solubility, the resultant fraction being designatedI-7 and having aclottability of about 95%. Reprecipitation of 1-7 with glycine was far less complete than anticipated, but yielded material consistently 97% or more clottable. This observed change in glycine precipitability of 1-7 was attributable to its relative Isolation from fibrinogen of lower solubility with which it appeared to interact. Solubility studies of Isolated fibrinogen subtractions (1-3 to 1-8) demonstrated clearly the differences between these fractions, though all fractions were heterogeneous. The biologic reactivity to thrombin of the various subtractions was directly related to their solubility; the higher the solubility, the longer the thrombin time.