title: Biosynthesis of lipid-linked oligosaccharides by microsomes from virus induced Hepatoma MC-29. Dependence of some glycosyl transferases on dolichyl phosphates of different chain length.
abstract: Dolichyl phosphates of various chain length ranging from 7 to 22 isoprene units were tested as lipid acceptors in transglycosylation reactions in chicken liver and Hepatoma MC-29. In the presence of exogenous dolichyl phosphate mixture (18 and 19 isoprene units) the synthesis of dolichyl pyrophosphate N-acetylglucosamine and dolichyl phosphate mannose increased 3 times both in the liver and Hepatoma MC-29, while the formation of dolichyl phosphate glucose was 4 fold higher in the liver and 6-fold higher in Hepatoma MC-29. In liver microsomes the maximum rate of the stimulation of glycosylation was achieved by exogenous dolichyl phosphates, containing 18 and 19 isoprene units, while glycosyl transferases in microsomes from Hepatoma MC-29 did not show any structural requirements to the chain length of dolichyl phosphates.
authors.forename: R T
authors.initials: RT
authors.lastname: Tosheva
authors.forename: L I
authors.initials: LI
authors.lastname: Stoykova
authors.forename: V I
authors.initials: VI
authors.lastname: Zhivkov
mesh_terms: D000818:Animals; D002645:Chickens; D004288:Dolichol Phosphates / Q000378:metabolism*; D005964:Glucosyltransferases / Q000378:metabolism*; D006602:Hexosyltransferases / Q000378:metabolism*; D008099:Liver / Q000378:metabolism; D008114:Liver Neoplasms, Experimental / Q000378:metabolism; D008364:Mannosyltransferases / Q000378:metabolism*; D008862:Microsomes, Liver / Q000378:metabolism*; D017351:N-Acetylglucosaminyltransferases; D011106:Polyisoprenyl Phosphates / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D004288:Dolichol Phosphates; D011106:Polyisoprenyl Phosphates; D005964:Glucosyltransferases; D006602:Hexosyltransferases; D008364:Mannosyltransferases; D017351:N-Acetylglucosaminyltransferases; C037649:N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase