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Thromb Haemost 1971; 26(03): 526-540
DOI: 10.1055/s-0038-1653706
Originalarbeiten – Original Articles – Travaux Originaux
Schattauer GmbH

A Comparative Study of Adult and Fetal Sheep Fibrinogen, Sulf-Fibrinogen and Fibrinogen Degradation Products

W Loly
1   Department of Pediatrics and Medicine, University of Manitoba and the Clinical Investigation Units of the Winnipeg Children’s Hospital and the Winnipeg General Hospital
,
L. G Israels
1   Department of Pediatrics and Medicine, University of Manitoba and the Clinical Investigation Units of the Winnipeg Children’s Hospital and the Winnipeg General Hospital
,
A. J Bishop   *)
1   Department of Pediatrics and Medicine, University of Manitoba and the Clinical Investigation Units of the Winnipeg Children’s Hospital and the Winnipeg General Hospital
,
E. D Israels
1   Department of Pediatrics and Medicine, University of Manitoba and the Clinical Investigation Units of the Winnipeg Children’s Hospital and the Winnipeg General Hospital
› InstitutsangabenThis study was supported by a grant from the Manitoba Heart Foundation.
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Publikationsdatum:
28. Juni 2018 (online)

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Summary

The results of these comparative studies of adult and fetal sheep fibrinogen are as follows:

1. Adult D fragments and sulf-fibrinogen are identical to their fetal counterparts when examined by acid alkaline polyacrylamide gel electrophoresis.

2. Adult and fetal E fragments show identical mobility on acid and alkaline polyacrylamide gel electrophoresis, but in the alkaline system the adult E piece consistently shows 3 separate bands while the fetal E peice, with one exception, is one diffuse band. The pattern of banding of the two E fragments is identical in the acid gel system.

3. Adult D and E fragments and sulf-fibrinogen are immunologically identical to their fetal counterparts.

4. Thrombin times on fetal plasmas are, on the average, prolonged over those on adult plasmas ; this is probably due to the lower absolute fibrinogen concentration of fetal plasma.

5. Adult and fetal fibrinogen showed no differences in the pH dependency of their thrombin times, indicating that the polymerization process is probably the same in both.

6. It is essential, in studies of fibrinogen structure and function, to work with very pure fibrinogen preparations, free from fibrin monomers and fibrinogen degradation products.

*) Centennial Fellow, Medical Research Council of Canada.


 

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