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Isolation of a fraction enriched in the trans-Golgi network from baby hamster kidney cells.

Abstract：

:Incubation of cultured cells at 20 degrees C blocks the transport of newly synthesized plasma membrane proteins, and the proteins accumulate intracellularly in a terminally glycosylated form. When baby hamster kidney cells are infected with the ts O45 mutant of vesicular stomatitis virus, and incubated at 20 degrees C, the terminally glycosylated spike glycoprotein G of the virus accumulates in the membranes of a tubular network localized on the trans side of the Golgi cisternae, the trans-Golgi network (TGN). We have used the G protein of ts O45 as a marker for the TGN and isolated a TGN fraction using a combination of conventional cell fractionation techniques and immunoisolation. The TGN was separated from the bulk of the endoplasmic reticulum, mitochondria, lysosomes, plasma membrane, and endosomes, while the activity of trans-Golgi marker galactosyltransferase copurified with the G protein. Using G protein as the TGN marker we have determined that the TGN was enriched 25-fold in the final fraction relative to the total homogenate. Several polypeptides (Mr 75,000, 87,000, 92,000, and 120,000) copurified with the G protein in the isolated TGN fraction and most likely represent resident markers of the compartment.

journal_name

Exp Cell Res

journal_title

Experimental cell research

authors

de Curtis I,Howell KE,Simons K

doi

10.1016/0014-4827(88)90190-5

subject

Has Abstract

pub_date

1988-04-01 00:00:00

pages

248-65

issue

2

eissn

0014-4827

issn

1090-2422

journal_volume

175

pub_type

杂志文章

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