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- W1011692429 abstract "Research Article1 March 1985free access Examination of calf prochymosin accumulation in Escherichia coli: disulphide linkages are a structural component of prochymosin-containing inclusion bodies. J.M. Schoemaker J.M. Schoemaker Search for more papers by this author A.H. Brasnett A.H. Brasnett Search for more papers by this author F.A. Marston F.A. Marston Search for more papers by this author J.M. Schoemaker J.M. Schoemaker Search for more papers by this author A.H. Brasnett A.H. Brasnett Search for more papers by this author F.A. Marston F.A. Marston Search for more papers by this author Author Information J.M. Schoemaker, A.H. Brasnett and F.A. Marston The EMBO Journal (1985)4:775-780https://doi.org/10.1002/j.1460-2075.1985.tb03696.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Recent reports have shown that synthesis of certain recombinant proteins in Escherichia coli results in the production of intracellular inclusion bodies. These studies have not analyzed the structure of the inclusion body especially regarding the intermolecular forces holding it together. We have examined structural aspects of inclusion bodies made in E. coli as a result of high level expression of the eukaryotic protein, calf prochymosin. Prochymosin is a monomeric protein containing three disulfide bridges. It was expressed at up to 20% of cell protein from a plasmid containing the E. coli tryptophan promoter, operator and ribosome binding site. Proteins in the inclusion bodies were analysed by Western blotting of SDS-polyacrylamide gels. When experiments were done using conditions which preserved the in vitro state of thiol groups, inclusions were shown to be composed of multimers of prochymosin molecules which were interlinked partly by disulfide bonds. The inclusion bodies also contained a high concentration of reduced prochymosin. The presence of intermolecular disulfides probably contributes to the difficulty of solubilizing recombinant prochymosin during its purification from E. coli. Previous ArticleNext Article Volume 4Issue 31 March 1985In this issue RelatedDetailsLoading ..." @default.
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- W1011692429 title "Examination of calf prochymosin accumulation in Escherichia coli: disulphide linkages are a structural component of prochymosin-containing inclusion bodies." @default.
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- W1011692429 doi "https://doi.org/10.1002/j.1460-2075.1985.tb03696.x" @default.
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