Bovine α2‐antiplasmin N‐Terminal and reactive site sequence

FEBS Letters

Christensen, Søren¹  Sottrup-Jensen, Lars¹ 

[1] Department of Molecular Biology, University of Aarhus, Building 130, 8000 Århus C, Denmark

关键词: Plasma protein;    Proteinase inhibitor;    Sequence analysis;    α2-Antiplasmin;    α2AP;    α2-antiplasmin;    serpin;    serine protease inhibitor;    DCI;    3;    4-dichloroisocoumarin;    CTA;    committee of thrombolytic agents;    ε-ACA;    ε-aminocaproic acid;    K;    kringle region of plasminogen;    HPLC;    high performance liquid chromatograph(y);    TFA;    trifluoroacetic acid;   

DOI  :  10.1016/0014-5793(92)81419-M

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Bovine α₂-antiplasmin (α₂AP) has been purified and partially characterized. The amino acid composition is very similar to that of human α₂AP, 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 α₂AP, bovine α₂AP has an 18-residue N-terminal extension, homologous with part of the pre-sequence of human α₂AP. A re-investigation of the N-terminal sequence of freshly prepared human α₂AP reveals a new form extended by 12 residues.

【 授权许可】

Unknown