N-Linked glycosylation of tissue plasminogen activator in Namalwa cells

Khan, Mohsan W.; Musgrave, S.C.; Jenkins, Nigel

doi:10.1042/bst023099s

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Protein Translation Quality Control and Covalent Modification1

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Cited by 4 publications

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“…Differences in glycosylation of a given protein are a result of divergence in the Golgi‐based processing of the oligosaccharides in different cell types (Jenkins et al, ). The human lymphoblastoid Namalwa cell line performs O‐ and N‐linked glycosylation of recombinant tPA efficiently to produce human‐type glycosylation characteristics (Okamoto et al, ; Khan et al, ). Most CHO cell lines used in production of recombinant proteins do not possess active α1,3‐galactosyltransferase, although the gene is present in these cells, which make low levels of galactosamine neuraminic acid.…”

Section: Protein Translation Quality Control and Covalent Modificationmentioning

confidence: 99%

Overview of Protein Expression by Mammalian Cells

Gray¹

1997

CP Protein Science

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This unit reviews the stages involved in protein production in mammalian cells using a stable-expression approach. Choice of cell type is discussed, as is transfection of the host cells, methods for selection and amplification of transformants, and growth of cells at appropriate scale for protein production. Since post-transcriptional modification and intracellular protein transportation are important features of recombinant-protein production in mammalian cells, some description of these mechanisms is included.

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Section: Protein Translation Quality Control and Covalent Modificationmentioning

confidence: 99%