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[治疗性血清蛋白溶液的抑制和免疫学特性]

[Inhibitory and immunological profile of therapeutic serum protein solutions].

作者信息

Kotitschke R, Stephan W

出版信息

Infusionsther Klin Ernahr. 1985 Feb;12(1):48-53.

PMID:3886542
Abstract

Biseko is prepared from pooled human plasma by specific stepwise adsorption of the coagulation factors avoiding spontaneous coagulation. Biseko is manufactured from pooled plasma from more than 1000 donors. In order to ensure its hepatitis safety, the starting plasma is cold sterilized by beta-propiolactone and UV-irradiation. The inhibitory and immunological profile of the cold sterilized Biseko was compared with another commercial serum preserve and normal serum. alpha 1-antitrypsin, alpha 2-macroglobulin and antithrombin III are present in Biseko and normal serum in their biologically active forms. A certain amount of the opsonin, fibronectin, is heparin-precipitable in normal serum and has thus retained its native character, while the fibronectin in the commercial serum preserve examined is not heparin-precipitable. Biseko contains fibronectin only in trace amounts. The IgG, IgA and IgM immunoglobulin concentrations and activities in the serum preserves are equivalent to those in normal serum. One major difference between normal serum and the cold sterilized Biseko is that metabolites from the coagulation pathways are absent in Biseko. Normal serum is not suitable for therapeutic purposes because of activated enzymes formed during coagulation. The chemical analysis of the protein pattern in Biseko resembles more fresh frozen plasma without coagulation factors than normal serum.

摘要

Biseko是通过对凝血因子进行特定的逐步吸附,从混合人血浆中制备而成,避免了自发凝血。Biseko由来自1000多名献血者的混合血浆制成。为确保其肝炎安全性,起始血浆用β-丙内酯和紫外线照射进行冷灭菌。将冷灭菌的Biseko的抑制和免疫学特征与另一种商业血清保存剂和正常血清进行了比较。α1-抗胰蛋白酶、α2-巨球蛋白和抗凝血酶III以其生物活性形式存在于Biseko和正常血清中。一定量的调理素纤维连接蛋白在正常血清中可被肝素沉淀,因此保留了其天然特性,而所检测的商业血清保存剂中的纤维连接蛋白则不能被肝素沉淀。Biseko仅含有微量的纤维连接蛋白。血清保存剂中的IgG、IgA和IgM免疫球蛋白浓度及活性与正常血清中的相当。正常血清与冷灭菌的Biseko之间的一个主要区别是,Biseko中不存在凝血途径的代谢产物。由于凝血过程中形成的活化酶,正常血清不适合用于治疗目的。Biseko中蛋白质模式的化学分析与不含凝血因子的新鲜冷冻血浆比与正常血清更相似。

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