The β-phosphoro[35 S]thioate analogue of UDP-Glc is efficiently utilized by the glucose phosphotransferase and is relatively resistant to hydrolytic degradation

Published

Journal Article

The β-phosphoro[35S]thioate analogue of UDP-glucose ((β-35S)UDP-Glc) is utilized with approximately the same efficiency as the parent compound by the UDP-glucose:glycoprotein glucose-1-phosphotransferase (glucosyltransferase), which catalyzes the transfer of αGlc-1-P from UDP-Glc to mannose-containing oligosaccharides on acceptor glycoproteins. The same endogenous acceptor glycoproteins are labeled by the glucosyltransferase using [β-32P]UDP-Glc and (β-35S)UDP-Glc. However, in liver homogenates, incorporation from [β-32P]UDP-Glc ceases to increases after about 4 min of incubation, while incorporation from (β-35S)UDP-Glc persists for at least 1 h. This difference is due to an approx. 10-fold slower hydrolytic rate for the phosphorothioate analogue than for the parent compound, a finding similar to previous work showing that a variety of nucleases and phosphodiesterases are less efficient in cleaving phosphorothioate DNA than the native polymer. © 1987.

Full Text

Duke Authors

Cited Authors

  • Marchase, RB; Saunders, AM; Rivera, AA; Cook, JM

Published Date

  • November 26, 1987

Published In

Volume / Issue

  • 916 / 2

Start / End Page

  • 157 - 162

International Standard Serial Number (ISSN)

  • 0167-4838

Digital Object Identifier (DOI)

  • 10.1016/0167-4838(87)90103-8

Citation Source

  • Scopus