Proteinase inhibitors from the tropical sea anemone Radianthus macrodactylus: isolation and characteristic

Biochemistry (Mosc). 2007 Mar;72(3):301-6. doi: 10.1134/s0006297907030078.

Abstract

Two new serine proteinase inhibitors (RmIn I and RmIn II) from the tropical sea anemone Radianthus macrodactylus have been isolated and characterized. The purification procedure includes polychrome-1 hydrophobic chromatography, Superdex Peptide 10/30 FPLC, and Nucleosil C(18) reverse-phase HPLC. The molecular masses of RmIn I, RmIn II, and the complexes RmIn II/trypsin and RmIn I,II/alpha-chymotrypsin have been determined. The K(i) values of RmIn I and RmIn II for trypsin and alpha-chymotrypsin have been determined. The polypeptides RmIn I and RmIn II are shown to be nontoxic and to exhibit antihistamine activity. The N-terminal amino acid sequences of RmIn I (GICSEPIVVGPCKAG-) and RmIn II (GSTCLEPKVVGPCKA-) have been determined. A high homology of the amino acid sequences is demonstrated for the proteinase inhibitors produced by such evolutionarily distant species as coelenterates, reptiles, and mammals.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chromatography, High Pressure Liquid
  • Chymotrypsin / antagonists & inhibitors
  • Chymotrypsin / metabolism
  • Kinetics
  • Mass Spectrometry
  • Molecular Sequence Data
  • Molecular Weight
  • Protease Inhibitors / chemistry*
  • Protease Inhibitors / isolation & purification*
  • Protease Inhibitors / pharmacology
  • Protein Isoforms / chemistry
  • Protein Isoforms / isolation & purification
  • Protein Isoforms / pharmacology
  • Sea Anemones / chemistry*
  • Sequence Analysis, Protein
  • Sequence Homology, Amino Acid
  • Trypsin / metabolism

Substances

  • Protease Inhibitors
  • Protein Isoforms
  • Chymotrypsin
  • Trypsin