Abstract:
:A higher level of N-acetylglucosamine incorporation by proteinic and polyprenic endogenous acceptors is observed after infection by Myxovirus. This phenomenon occurs in whole mitochondria as in outer mitochondrial membranes, where it is particularly obvious with proteinic endogenous acceptors. Under viral infection, no new N-acetylglucosaminylated polyprenol is detected. In the case of infected animals as in the case of control animals, compounds P1 (extracted by chloroform/methanol 2:1) are identified by thin layer chromatography as a N-acetylglucosamyl-pyrophosphoryl-dolichol and a N, N'-diacetylchitobiosyl-pyrophosphoryl-dolichol. In the case of infected animals, biosynthesis of proteinic acceptors and dolichol is not modified; therefore the increase of N-acetylglucosamine incorporation is not due to a modification of the endogenous acceptors level. By the use of exogenous dolichol-monophosphate we demonstrate that the increased transfer of [14C] N-acetylglucosamine into polyprenic acceptors is the result of a higher activity of the mitochondrial N-acetylglucosaminyltransferase after viral infection.
journal_name
Biochimiejournal_title
Biochimieauthors
Gateau O,Morelis R,Louisot Pdoi
10.1016/s0300-9084(80)80373-7subject
Has Abstractpub_date
1980-01-01 00:00:00pages
79-84issue
1eissn
0300-9084issn
1638-6183pii
S0300-9084(80)80373-7journal_volume
62pub_type
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