Porcine tissue plasminogen activator

FEBS Letters

Kok, Preben¹  Wallén, Per¹  Jörnvall, Hans¹  Pohl, Gunnar¹ 

[1] Department of Physiological Chemistry, Umeå University S-901 87 Umeå and Department of Chemistry I, Karolinska Institutet, S-104 01 Stockholm, Sweden

关键词: Amino acid sequence analysis;    Endoglycosidase treatment;    Electrophoresis;   

DOI  :  10.1016/0014-5793(86)80872-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Tissue plasminogen activator was purified in high yield from pig heart by immunoaffinity chromatography and characterized by analysis of the glycosylation pattern and the N-terminal amino acid sequence. Comparisons with the human enzyme reveals residue exchanges in the A-chain at positions 3 (porcine Arg/human Gin) and 5 (Thr/Ile), and in the B-chain at positions 6 (Tyr/Phe), 10 (Thr/Ala) and 20 (Val/Ala). The glycosylation pattern for the porcine activator was determined by endoglycosidase treatment followed by gel electrophoresis. The A-chain contains a single high-mannose type of JV-linked glycan structure and the B-chain contains a complex type of oligosaccharide. A similar but not identical pattern has been observed for the human activator, purified from melanoma cells.

【 授权许可】

Unknown