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- W2016142807 abstract "cDNA analysis has revealed that the 50 amino acid transforming growth factor-alpha (TGF-alpha) is derived from a 160 amino acid precursor. Antibodies to TGF-alpha and to a C-terminal portion of the precursor were used to study the biosynthesis and processing of the precursor. CHO cells transfected with a TGF-alpha expression vector secrete high levels of TGF-alpha; a mixture of species of about 18 kd is secreted in addition to the 50 amino acid form. These larger species are N-glycosylated and are derived from the same precursor as the smaller form. The C-terminal segment of the precursor remains anchored in the membrane and has covalently attached palmitate. The newly synthesized TGF-alpha precursor is thus a transmembrane protein that subsequently undergoes external proteolytic cleavages, releasing several TGF-alpha species." @default.
- W2016142807 created "2016-06-24" @default.
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- W2016142807 date "1987-02-01" @default.
- W2016142807 modified "2023-09-25" @default.
- W2016142807 title "Different transforming growth factor-α species are derived from a glycosylated and palmitoylated transmembrane precursor" @default.
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- W2016142807 doi "https://doi.org/10.1016/0092-8674(87)90194-2" @default.
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