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. 1982 Mar;69(3):678–681. doi: 10.1104/pp.69.3.678

Glycoprotein Biosynthesis in Chlamydomonas1

I. IN VITRO INCORPORATION OF GALACTOSE FROM UDP-[14C]GALACTOSE INTO MEMBRANE-BOUND PROTEIN

Winfried C Lang 1
PMCID: PMC426279  PMID: 16662274

Abstract

A crude membrane fraction from Chlamydomonas reinhardii was found to catalyze d-galactose transfer from UDP-galactose to endogenous proteins. Highest incorporation rates were achieved by incubation at 25°C and pH 7.5 in the presence of 10 millimolar Fe2+. Hydrolytic studies on the labeled polymer revealed that radioactivity was attached to protein via an alkali-stable and acid-labile linkage. Identification of galactose as the only labeled sugar in the acid hydrolysate and results of a tentative estimation of the molecular weight of the charged alkaline degradation product indicate that monomeric galactose units are transferred to form an O-glycosidic bond with peptidyl hydroxyproline. No indications were found for a similar linkage to serine which, in contrast to the hydroxyproline-O-glycoside linkage, is acid-stable but is cleaved by β-elimination. Chromatography of the sodium dodecyl sulfate-solubilized polymer on Sepharose-6B demonstrated that galactosyl residues are mainly associated with proteins which are of considerably higher molecular weight than are the majority of sodium dodecyl sulfate-denatured membrane proteins in this fraction.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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