Thromb Haemost 1969; 21(03): 409-418
DOI: 10.1055/s-0038-1653555
Originalarbeiten - Original Articles - Travaux Originaux
Schattauer GmbH

Bovine Platelet Proteins

I. Soluble Proteins Studied by Immunoelectrophoresis and Polyacrylamide Disc Electrophoresis
S Łopaciuk1)
1   Institute for Thrombosis Research, Rikshospitalet, Oslo 1, Norway
,
N. O Solum
1   Institute for Thrombosis Research, Rikshospitalet, Oslo 1, Norway
› Author Affiliations
Further Information

Publication History

Publication Date:
10 June 2018 (online)

Summary

1. The protein composition of bovine platelet extracts has been investigated by immunoelectrophoresis and polyacrylamide disc electrophoresis. The information obtained is discussed as a basis for study on platelet fibrinogen.

2. With antiserum to platelet proteins 11 precipitin lines were observed 3 of which corresponded electrophoretically to plasma albumin, fibrinogen and γ-globulin. These lines were not seen using the same antiserum absorbed with bovine plasma. The 8 additional lines were still present indicating that they represented specific platelet components. Antiserum to plasma produced the 3 above-mentioned lines, but no others.

3. With antiserum to purified bovine plasma fibrinogen 3 precipitin lines were observed. The fibrinogen line was the dominant one. The 2 additional lines did not disappear by absorption of the antiserum with bovine serum nor by incubation of the extracts with thrombin. The latter treatment totally removed the fibrinogen line.

4. A non-fibrinogen precipitin line, observed only with the antiserum to platelet extract and positioned in the β2-globulin region, disappeared by the incubation of platelet extracts with thrombin.

1) On WHO fellowship. Permanent adress: Institute of Haematology, Chocimska 5, Warsaw Poland.


 
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