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• W1863234733 abstract "Research Article1 December 1985free access Molecular cloning of S-protein, a link between complement, coagulation and cell-substrate adhesion. D. Jenne D. Jenne Search for more papers by this author K.K. Stanley K.K. Stanley Search for more papers by this author D. Jenne D. Jenne Search for more papers by this author K.K. Stanley K.K. Stanley Search for more papers by this author Author Information D. Jenne and K.K. Stanley The EMBO Journal (1985)4:3153-3157https://doi.org/10.1002/j.1460-2075.1985.tb04058.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info cDNA clones coding for human S-protein have been isolated using monoclonal antibodies to screen a cDNA library in pEX. These clones are shown to be authentic S-protein clones on the basis of sequence, composition and immunological criteria. The complete open reading frame sequence for S-protein has been determined and shows it to be a single polypeptide chain of 459 amino acids preceded by a cleaved leader peptide of 19 residues. No evidence was found for polymorphism of S-protein suggesting that different molecular weight forms arise by proteolytic degradation. Of the first 44 amino-terminal residues 42 are identical with the so-called somatomedin B peptide suggesting that S-protein is the somatomedin B precursor. Striking homology is found in the rest of the sequence with the serum spreading factor, vitronectin, which has also been shown to contain somatomedin B sequences at its amino terminus. We conclude that S-protein and vitronectin are identical and discuss the relevance of this finding to the coagulation and complement pathways. Previous ArticleNext Article Volume 4Issue 121 December 1985In this issue RelatedDetailsLoading ..." @default.
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• W1863234733 date "1985-12-01" @default.
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• W1863234733 title "Molecular cloning of S-protein, a link between complement, coagulation and cell-substrate adhesion." @default.
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• W1863234733 doi "https://doi.org/10.1002/j.1460-2075.1985.tb04058.x" @default.
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