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Plant and Cell Physiology, 1982, Vol. 23, No. 7 1259-1266
© 1982

Article

Glycoprotein Biosynthesis in Chlamydomonas II. No Evidence for Lipid Intermediates in Protein Galactosylation

Winfried C. Lang

Fachbereich Biologie der Universität Kaiserslautern Postfach 3049, 6750 Kaiserslautern, Federal Republic of Germany

A crude membrane fraction from Chlamydomonas reinhardii transferred radioactivity from UDP-[14C]galactose to endogenous lipids. Most of the radioactivity was detected in digalactosyl diacylglycerol moieties in which only the distal galactose residue ({alpha}-linked to monogalactosyl diacylglycerol) was labeled. A second compound was identified as monogalactosyl diacylglycerol labeled in the galactose moiety ß-linked to glycerol. In addition to these two galactolipid species, trace amounts of radioactive glucose were detected in the aqueous phase after mild acid treatment of the total lipid fraction. This demonstrates the presence of a 4-epimerase and provides indirect evidence for the presence of a small amount of polyprenyl-monophosphate-glucose which was presumably not detectable per se because of the bulk of neutral galactolipids. The failure to detect polyprenyl-phosphate-galactose or mild acid labile galactose at any time during the incubation suggests that galactosylation of Chlamydomonas proteins might occur without the involvement of lipid intermediates.

(Received May 10, 1982; Accepted August 21, 1982)
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