The rate of activation by urokinase of porcine plasminogen is accelerated by 6-aminohexanoate, although the maximally enhanced rate is 10-fold less than that of human plasminogen without the amino acid. 6-Aminohexanoate facilitates only activation of native porcine plasminogen (asp-plasminogen), but has no effect on activation of des-kringle1-4-plasminogen. Sodium chloride, on the other hand, inhibits activation by urokinase of both porcine asp-plasminogen and des-kringle1-4-plasminogen. It is concluded that 6-aminohexanoate exerts its effect via kringle1-4 domains of plasminogen, whereas CI- acts, at least in part, through effects on the kringle5 or proteinase domains.
|Number of pages||3|
|Journal||Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular|
|Publication status||Published - aug. 1 1990|
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology