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Heparin binding peptides co-purify with glycosaminoglycans from human plasma
M Chevanne1, R Caldini, G Manao
1Department of Experimental Pathology and Oncology, University of Firenze, Viale Morgani 50, 50134, Florence, Italy.
FEBS Letters
|December 22, 1999
Summary
Plasma glycosaminoglycans (GAGs) were investigated, revealing heparin-like GAGs associated with proteins. Despite dialysis, some GAGs remained bound, suggesting complex interactions within plasma components.
Area of Science:
- Biochemistry
- Proteomics
- Glycobiology
Background:
- Plasma contains glycosaminoglycans (GAGs) complexed with proteins.
- Understanding these interactions is crucial for plasma physiology.
Purpose of the Study:
- To investigate the nature and association of GAGs within human plasma.
- To identify specific GAGs present and their binding partners.
Main Methods:
- Proteolysis of plasma followed by gradient polyacrylamide gel electrophoresis (PAGE).
- Dialysis with a 3.5 kDa molecular weight cut-off.
- Analysis of peptide aggregation and heparin binding.
Main Results:
- Proteolysis significantly reduced the protein-GAG ratio, indicating strong protein-GAG complexes.
- Heparinase-1 sensitive GAGs were detected, suggesting the presence of heparin.
- High molecular weight peptide bands appeared on both sides of the dialysis membrane, indicating aggregation of low molecular weight peptides.
Conclusions:
- Human plasma contains heparin-like GAGs bound to proteins.
- Low molecular weight peptides can aggregate, complicating separation by dialysis.
- These aggregated peptides also exhibit heparin-binding properties.