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

Raymund Machovich, Whyte G. Owen

Research output: Contribution to journalArticle

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

Fingerprint

Aminocaproates
Plasminogen
Urokinase-Type Plasminogen Activator
Chlorides
Swine
Chemical activation
Ions
Sodium Chloride
Peptide Hydrolases

Keywords

  • 6-aminohexanoate
  • Chloride ion
  • Plasminogen
  • Urokinase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Structural Biology

Cite this

6-Aminohexanoate and chloride ion in the activation by urokinase of porcine plasminogens. / Machovich, Raymund; Owen, Whyte G.

In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 1040, No. 1, 01.08.1990, p. 109-111.

Research output: Contribution to journalArticle

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