Lijnen H R, Wiman B, van Hoef B, Collen D
Thromb Res. 1982 Jul 1;27(1):83-9. doi: 10.1016/0049-3848(82)90281-x.
Human alpha 2-antiplasmin was digested with CNBr and the partial NH2-terminal amino acid sequences of nine purified fragments were determined. One of these sequences (12 residues) revealed homologies with that of residues 158 to 168 and with that of residues 316-327 in the antithrombin III sequence and with the corresponding sequences in alpha 1-antitrypsin and ovalbumin. One CNBr-fragment of 69 residues with blocked NH2-terminus was subdigested with trypsin and chymotrypsin and most of its sequence aligned. This peptide probably represents the major part of the previously reported COOH-terminal fragment of alpha 2-antiplasmin with Mr 8,000 (1). In this sequence no clear homology with antithrombin III, alpha 1-antitrypsin or ovalbumin could be detected.
人α2-抗纤溶酶用溴化氰消化，并测定了九个纯化片段的部分NH2-末端氨基酸序列。其中一个序列（12个残基）显示与抗凝血酶III序列中158至168位残基以及316 - 327位残基的序列同源，也与α1-抗胰蛋白酶和卵清蛋白中的相应序列同源。一个含有69个残基且NH2-末端封闭的溴化氰片段用胰蛋白酶和糜蛋白酶进行了进一步消化，并确定了其大部分序列。该肽可能代表了先前报道的分子量为8000的α2-抗纤溶酶COOH-末端片段的主要部分（1）。在这个序列中，未检测到与抗凝血酶III、α1-抗胰蛋白酶或卵清蛋白的明显同源性。
