title: Porcine tissue plasminogen activator. Immunoaffinity purification, structural properties and glycosylation pattern.
abstract: 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 Gln) 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 N-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.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D006027:Glycosides / Q000378:metabolism; D006801:Humans; D009206:Myocardium / Q000032:analysis; D013045:Species Specificity; D013552:Swine; D010959:Tissue Plasminogen Activator / Q000302:isolation & purification*
chemical_list: D006027:Glycosides; D010959:Tissue Plasminogen Activator