Abstract
An mRNA fraction from dog liver translated with a rabbit reticulocyte protein synthesizing system in the presence of [ 35S]-methionine produces fibrinogen-related proteins which are immunoprecipitated with rabbit antiserum to dog fibrinogen. Analyses of these radioactive proteins by sodium dodecyl sulfate polyacrylamide gel electrophoresis and autoradiography indicate that the three fibrinogen chains (Aα, Bβ and γ) are synthesized separately as larger precursors. The putative pre Aα and pre Bβ chains were characterized by their susceptibility to treatment with thrombin and batroxobin. Thrombin degraded the pre Aα and pre Bβ chains, while batroxobin only acted on the pre Aα chain. The pre γ chain was not degraded by these enzymes.
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