Pepper D S, Banhegyi D, Cash J D
Thromb Haemost. 1977 Aug 31;38(2):494-503.
Antithrombin III (AT III) complexes were isolated from human serum by affinity chromatography and gel filtration. In the first step of the preparation, using heparin-agarose chromatography, we observed that the complexed form of AT III bound less strongly to the gel than the free form and that about half of the AT III was free. With further purification a 2.5 X 10(5) molecular weight complex was isolated. Using 125I labelled human thrombin, this complex was radioactive indicating the presence of thrombin. Only in a synthetic thrombin-AT III system was a 9 X 10(4) molecular weight complex detected, but not in serum. These facts suggest that in serum AT III complexes may exist in a polymeric form. Also, an AT III antigen derived from the original AT III molecule, but not complexed, was isolated which may be a degradation product.
通过亲和层析和凝胶过滤从人血清中分离抗凝血酶III（AT III）复合物。在制备的第一步，使用肝素琼脂糖层析，我们观察到与游离形式相比，AT III的复合形式与凝胶的结合较弱，并且大约一半的AT III是游离的。经过进一步纯化，分离出了分子量为2.5×10⁵的复合物。使用¹²⁵I标记的人凝血酶，该复合物具有放射性，表明存在凝血酶。仅在合成的凝血酶-AT III系统中检测到分子量为9×10⁴的复合物，而在血清中未检测到。这些事实表明，在血清中AT III复合物可能以聚合形式存在。此外，还分离出了源自原始AT III分子但未复合的AT III抗原，它可能是一种降解产物。
