STB LifeSaving Technologies and the American Red Cross, Holland Laboratory, Rockville, Maryland 20855, USA.
Transfusion. 2013 Mar;53(3):651-4. doi: 10.1111/j.1537-2995.2012.03778.x. Epub 2012 Jul 15.
On rare occasions, upon thawing of stored cryoprecipitate components, clots are observed on visual inspection. Although it has been assumed that the clot reflects fibrinogen to fibrin conversion, there are few published studies that document that this assumption is correct. Our studies were conducted to further identify the protein characteristics of the clotted material.
Clotted material isolated from four thawed cryoprecipitate pools was examined by solubilization procedures and electrophoresis analysis.
Solubilization of much of the clotted material in phosphate-buffered saline warmed to 37°C suggested the presence of soluble fibrin. Gel electrophoresis under reducing conditions showed that the most prevalent bands exhibited molecular weights corresponding to the α, β, and γ subunits of fibrinogen with a much lighter band exhibiting the molecular weight of fibrinogen γ-γ dimer, consistent with the presence of partially crosslinked fibrin. The presence of the dimer indicated that the clotted material was caused by the action of thrombin, but also reflected the action of Factor XIIIa. No ongoing clot formation was observed.
Our studies indicate that, on rare occasions, fibrinogen conversion to fibrin is responsible for observable clots in thawed cryoprecipitate pools. These clots are structurally heterogeneous, including both noncrosslinked (soluble) and crosslinked (insoluble) fibrin. This diversity in the fibrin structure may account for some of the diversity in the limited literature regarding their presence in cryoprecipitate pools.
在极少数情况下，储存的冷沉淀成分解冻后，肉眼观察到有凝块。尽管人们认为凝块反映了纤维蛋白原向纤维蛋白的转化，但很少有发表的研究证明这一假设是正确的。我们的研究旨在进一步确定凝块物质的蛋白质特征。
从四个解冻的冷沉淀池分离的凝块物质通过溶解程序和电泳分析进行检查。
在 37°C 温育的磷酸盐缓冲液中溶解大部分凝块物质表明存在可溶性纤维蛋白。在还原条件下的凝胶电泳显示，最常见的带表现出与纤维蛋白原的α、β和γ亚基相对应的分子量，而一个较轻的带表现出纤维蛋白原γ-γ二聚体的分子量，这与部分交联的纤维蛋白的存在一致。二聚体的存在表明凝块物质是由凝血酶引起的，但也反映了因子 XIIIa 的作用。未观察到正在进行的凝块形成。
我们的研究表明，在极少数情况下，纤维蛋白原向纤维蛋白的转化是解冻的冷沉淀池中可观察到凝块的原因。这些凝块在结构上是异质的，包括未交联（可溶性）和交联（不溶性）纤维蛋白。纤维蛋白结构的这种多样性可能解释了关于其在冷沉淀池中的存在的有限文献中的一些多样性。
