The krigle 4 domain of chicken plasminogen

Marianne Gyenes, László Patthy

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

The kringle 4 unit of chicken plasminogen is similar to mammalian kringle 4 domains in possessing a lysine-binding site. Chicken kringle 4 shows 73-77% sequence identity with the fourth kringle units of porcine, bovine and human plasminogens. A major difference between mammalian and chicken kringle 4 species is that in the latter a glucosamine-based carbohydrate substituent is linked to asparagine-34. Complexation of this carbohydrate with concanavalin A does not interfere with the binding of kringle 4 to lysine-Sepharose, suggesting that in the kringle-fold the glycosylated region is distant from the entrance of the lysine-binding pocket.

Original languageEnglish
Pages (from-to)326-330
Number of pages5
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume832
Issue number3
DOIs
Publication statusPublished - Dec 20 1985

Keywords

  • (Chicken)
  • Amino acid sequences
  • Kringle 4 domain
  • N-Glycosylation
  • Plasminogen

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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