Interaction of polyamines with proteins of human plasma: a preferential aggregation of fibrinogen and fibronectin (cold insoluble globulin).
The polyamines spermine and spermidine were found to aggregate proteins from human plasma and serum, apparently due to electrostatic interactions between these cations and anionic proteins. Fibrinogen and fibronectin (cold insoluble globulin) were identified as the major molecular components of aggregates, and fibronectin could be quantitatively removed from plasma by aggregation with spermine. The results indicate that fibrinogen and fibronectin have anionic groups which react with polyamines and which are essential for the solubility of these proteins.
D001798:Blood Proteins / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism; D005353:Fibronectins / Q000097:blood; D006801:Humans; D011073:Polyamines / Q000494:pharmacology*; D013095:Spermidine / Q000494:pharmacology; D013096:Spermine / Q000494:pharmacology
D001798:Blood Proteins; D005353:Fibronectins; D011073:Polyamines; D013096:Spermine; D005340:Fibrinogen; D013095:Spermidine