Chromatographie and Electrophoretic Properties of Synthetic Human Fibrinopeptides
Robin McKenzie
1
University Department of Respiratory Diseases, City Hospital, Edinburgh, and the South-East Scotland Regional Blood Transfusion Service, Royal Infirmary of Edinburgh
,
D. S Pepper
1
University Department of Respiratory Diseases, City Hospital, Edinburgh, and the South-East Scotland Regional Blood Transfusion Service, Royal Infirmary of Edinburgh
,
A. B Kay
1
University Department of Respiratory Diseases, City Hospital, Edinburgh, and the South-East Scotland Regional Blood Transfusion Service, Royal Infirmary of Edinburgh
Some properties of synthetic human fibrinopeptides were studied by thin-layer chromatography, thin-layer electrophoresis and low voltage and high voltage paper electrophoresis. The Rf values and electrophoretic mobilities of the peptides in these systems were determined. In high voltage electrophoresis synthetic and natural (fibrinogen-derived) peptides migrated in an identical fashion.
When gel filtration was performed in 0.05 M pyridine or 0.1 N ammonia, synthetic fibrinopeptides A and B appeared to be aggregated. In contrast, when filtration was performed in 1.3 M formic acid, the peptides eluted in positions corresponding to their monomeric molecular weights.
In addition it was possible to quantitate synthetic fibrinopeptides by two colorimetric assays, the Sakaguchi reaction and the Folin-Ciocalteu method. Ultraviolet extinction coefficients for each peptide were also determined.
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