Preparation and characterization of pig plasma and platelet gelsolins

Eur J Biochem. 1986 Nov 17;161(1):69-76. doi: 10.1111/j.1432-1033.1986.tb10125.x.


Pig plasma gelsolin has been prepared by a revised method involving poly(ethylene glycol) precipitation, chromatography on CM-cellulose and affinity chromatography on actin-Sepharose. Pig platelet gelsolin has been prepared by chromatography on DEAE-cellulose and actin-Sepharose. Partial chemical and proteolytic cleavage shows that the two proteins are closely related in their fragmentation patterns. The amino acid sequences are identical at the N-terminus of the platelet protein, but the plasma protein has an additional nine residues on the N-terminal side of the common sequence. Calcium binding studies show that the plasma protein has similar calcium binding properties to both macrophage and platelet gelsolins.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Blood Platelets / metabolism*
  • Calcium / metabolism
  • Calcium-Binding Proteins / blood*
  • Catalysis
  • Chromatography / methods
  • Electrophoresis, Polyacrylamide Gel
  • Ethylene Glycol
  • Ethylene Glycols
  • Gelsolin
  • Microfilament Proteins / blood*
  • Peptide Chain Termination, Translational
  • Swine


  • Calcium-Binding Proteins
  • Ethylene Glycols
  • Gelsolin
  • Microfilament Proteins
  • Ethylene Glycol
  • Calcium