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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Pohl G,Jörnvall H,Kok P,Wallén Pdoi
10.1016/0014-5793(86)80872-9subject
Has Abstractpub_date
1986-09-01 00:00:00pages
92-6issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(86)80872-9journal_volume
205pub_type
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