Christensen S, Sottrup-Jensen L
Department of Molecular Biology, University of Aarhus, Denmark.
FEBS Lett. 1992 Nov 2;312(1):100-4. doi: 10.1016/0014-5793(92)81419-m.
Bovine alpha 2-antiplasmin (alpha 2AP) has been purified and partially characterized. The amino acid composition is very similar to that of human alpha 2AP, and the N-terminal (23 residues determined) and reactive site loop sequences (42 residues determined) are highly homologous to those of the human protein. Compared with human alpha 2AP, bovine alpha 2AP has an 18-residue N-terminal extension, homologous with part of the pre-sequence of human alpha 2AP. A re-investigation of the N-terminal sequence of freshly prepared human alpha 2AP reveals a new form extended by 12 residues.
牛α2-抗纤溶酶(α2AP)已被纯化并进行了部分特性鉴定。其氨基酸组成与人类α2AP非常相似,N端(已确定23个残基)和反应位点环序列(已确定42个残基)与人类蛋白质的高度同源。与人类α2AP相比,牛α2AP有一个18个残基的N端延伸,与人类α2AP前序列的一部分同源。对新制备的人类α2AP的N端序列重新研究发现了一种新的形式,其延伸了12个残基。