Aberrant O-glycosylation in the collagenous domain of pro alpha2(I) procollagen subunits synthesized by chemically transformed hamster fibroblasts

Chemically transformed Syrian hamster embryo fibroblasts (NQT-SHE) do not synthesize the pro alpha1(I) subunit of type I collagen, but they secrete two forms of the pro alpha2(I) subunit (N33 and N50) with abnormal post-translational modifications localized in the alpha2CB3,5 cyanogen bromide peptid...

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Veröffentlicht in:	Archives of biochemistry and biophysics 1997-06, Vol.342 (1), p.29-37
Hauptverfasser:	Ramachandran, U, Peterkofsky, B
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylgalactosamine - analogs & derivatives Animals Benzyl Compounds Binding Sites Brefeldin A Cell Line, Transformed Collagen - chemistry Collagen - metabolism Cricetinae Cyclopentanes - pharmacology Enzyme Inhibitors Glycoside Hydrolases Glycosylation Isoelectric Focusing Monensin - pharmacology Procollagen - chemistry Procollagen - metabolism
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