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Bovine α2‐antiplasmin N‐Terminal and reactive site sequence
[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.

[发布日期]  [发布机构] 
[效力级别]  [学科分类] 生物化学/生物物理
[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 [时效性] 
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