Lijnen H R, Wiman B, Collen D
Thromb Haemost. 1982 Dec 27;48(3):311-4.
Human alpha 2-antiplasmin was digested with trypsin and with chymotrypsin and about 70 percent of the amino acids were sequenced and aligned in peptides ranging from 2 to 33 residues. Here we report five sequences of 21 to 33 residues. When these were compared with the primary structures of antithrombin III, alpha 1-antitrypsin and ovalbumin, which belong to the same protein superfamily (Hunt and Dayhoff [1980] Biochem Biophys Res Commun 95: 864-871), three peptides showed clear homologies with these proteins, indicating that alpha 2-antiplasmin also belongs to that superfamily. In addition, alpha 2-antiplasmin appeared to contain at least one internal homology.
人α2-抗纤溶酶用胰蛋白酶和糜蛋白酶消化，约70%的氨基酸被测序并排列成2至33个残基的肽段。在此我们报告5个21至33个残基的序列。当将这些序列与抗凝血酶III、α1-抗胰蛋白酶和卵清蛋白的一级结构进行比较时（它们属于同一蛋白质超家族，Hunt和Dayhoff [1980] 《生物化学与生物物理研究通讯》95: 864 - 871），三个肽段与这些蛋白质显示出明显的同源性，表明α2-抗纤溶酶也属于该超家族。此外，α2-抗纤溶酶似乎含有至少一个内部同源性。
