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Abstract
Glycopeptides derived from surface and subcellular membranes of control (BHK21/C13) and virus-transformed (C13/B4) baby hamster kidney cells treated or untreated with ethidium bromide were studied. Ethidium bromide was found to mimic virus transformation with regard to the alteration of the glycopeptide patterns observed upon Sephadex G-50 chromatography. Elution profiles of glycopeptides obtained from virus-transformed cells demonstrated the existence of both a normal component (Peak B) and an enrichment of material eluting as a higher molecular weight component (Peak A). Material eluting in the Peak A region is greatly enhanced in both the control and virus-transformed cells after treatment with ethidium bromide. This alteration of the glycopeptide pattern was observed with glycopeptides derived from surface, endoplasmic reticular and mitochondrial membranes. Mitochondrial glycopeptides obtained from ethidium bromide-treated cells also seem to contain an increased amount of material eluting as a component of lower molecular weight than Peak B. This material, designated Peak C, may be located in the intramembrane space of the mitochondrion.
Highlights
MethodsCell Culture and Cell FractionationBaby hamster kidney cells (BHKtl/CIJ and the same cells transformed with the Bryan strain of Itous sarcoma virus (CIJBd) were cultured under previously defined conditions (l-3)
Elution profiles of glycopeptides obtained from virus-transformed cells demonstrated the existence of both a normal component (Peak B) and an enrichment of material eluting as a higher molecular weight component
Glycopeptides derived from surface and subcellular membranes of control (BHK2,/C13) and virus-transformed (CIS/B1)
Summary
Cell Culture and Cell FractionationBaby hamster kidney cells (BHKtl/CIJ and the same cells transformed with the Bryan strain of Itous sarcoma virus (CIJBd) were cultured under previously defined conditions (l-3). Control cells were grown in roller bottles for 3 days in the presence of. The untreated transformed cells were grown for 3 days in the presence of L-[3H]fucose. Cells were harvested from the roller bottles by incubation for 5 min with trypsin (0.25oj, Trypsin-Difco, 1:250 in Tris buffered saline, pH 7.5, with 0.1 M E:DTA) and centrifuged as previously described (l-3) to obtain a cell pellet and a supernatant. This supernatant contained surface components of the cells and was termed the cell trypsinate. The glycopeptides contained in the trypsinate are representative of those found in the plasma membrane as a whole (1, 2)
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