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Thromb Haemost 1982; 47(01): 019-021
DOI: 10.1055/s-0038-1657116
Original Article
Schattauer GmbH Stuttgart

Sialic Acid Dependent Polypeptide Chain Heterogeneity of Human Fibrinogen Demonstrated by Two-Dimensional Electrophoresis

Cemal Kuyas
The Thrombosis Research Laboratory, University Department of Medicine, Inselspital, Berne, Switzerland
,
André Haeberli
The Thrombosis Research Laboratory, University Department of Medicine, Inselspital, Berne, Switzerland
,
P Werner Straub
The Thrombosis Research Laboratory, University Department of Medicine, Inselspital, Berne, Switzerland
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Publikationsverlauf

Received 07. September 1981

Accepted 02. Dezember 1981

Publikationsdatum:
13. Juli 2018 (online)

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Summary

Human fibrinogen was compared with asialofibrinogen by two-dimensional electrophoresis to evaluate the contribution of sialic acid to the heterogeneity of the γ- and Bβ-polypeptide chains.

Reduced fibrinogen showed three major variants for both the γ- and Bβ-chains. In addition two minor γ-bands with a more acidic isoelectric point than the normal γ-chains were observed. Electrophoresis in the second dimension (SDS) suggests that these most acidic bands are γ-chain-variants with a higher molecular weight. In asialofibrinogen only two predominant variants with more alkaline isoelectric points were present in each chain type.

It is concluded that enzymatic removal of sialic acid partially reduces the heterogeneity of the γ- and Bβ-polypeptide chains of human fibrinogen, but additional sources producing charge heterogeneity must be sought.

Key words

Key words Fibrinogen - Heterogeneity - Sialic acid - Two-dimensional electrophoresis
 

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