Biochemistry (Moscow)

, Volume 69, Issue 7, pp 770–775 | Cite as

Protein Profiling of the Medicinal Leech Salivary Gland Secretion by Proteomic Analytical Methods

  • I. P. Baskova
  • L. L. Zavalova
  • A. V. Basanova
  • S. A. Moshkovskii
  • V. G. Zgoda
Article

Abstract

Protein diversity of the high molecular weight fraction (molecular mass > 500 daltons) of salivary grand secretion of the medicinal leech Hirudo medicinalis has been demonstrated using methods of proteomic analysis. One-dimensional (1D) electrophoresis revealed the presence of more than 60 bands corresponding to molecular masses ranging from 11 to 483 kD. 2D-electrophoresis revealed more than 100 specific protein spots differing in molecular masses and pI values. SELDI-mass spectrometry analysis using the ProteinChip System based on chromatography surfaces of strong anion or weak cation exchanger detected 45 individual compounds of molecular masses ranged from 1.964 to 66.5kD. Comparison of SELDI-MS data with protein databases revealed eight known proteins from the medicinal leech. Other masses detected by proteomic analytical methods may be related to both modifications of known proteins and unknown biologically active components of leech saliva secretion.

medicinal leech salivary gland secretion proteomics 1D-electrophoresis 2D-electrophoresis protein chip SELDI-MS 

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Copyright information

© MAIK “Nauka/Interperiodica” 2004

Authors and Affiliations

  • I. P. Baskova
  • L. L. Zavalova
  • A. V. Basanova
  • S. A. Moshkovskii
    • 1
  • V. G. Zgoda
    • 1
  1. 1.Orekhovich Institute of Biomedical ChemistryRussian Academy of Medical SciencesMoscowRussia

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