6-Aminohexanoate and chloride ion in the activation by urokinase of porcine plasminogens

Raymund Machovich, Whyte G. Owen

Research output: Article

5 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)109-111
Number of pages3
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume1040
Issue number1
DOIs
Publication statusPublished - aug. 1 1990

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of '6-Aminohexanoate and chloride ion in the activation by urokinase of porcine plasminogens'. Together they form a unique fingerprint.

  • Cite this