Galactosyltransferase activity of the microvillous surface of human placental syncytial trophoblast

D. M. Nelson, A. C. Enders, B. F. King

Research output: Contribution to journalArticle

6 Scopus citations


The syncytial trophoblast has previously been shown to have minimal intrasyncytial galactosyltransferase activity at term. The biochemical and autoradiographic study reported here shows that the microvillous surface of term human placental syncytial trophoblast has a galactosyltransferase activity capable of transferring 3H-galactose from uridine diphosphate-D-galactose-1-3H to trichloroacetic-acid-precipitable, endogenous acceptors. This capability of resynthesizing cleaved galactose moieties in the glycocalyx, without dependence on cytoplasmically located galactosyltransferases, would allow for reinstatement of the original surface molecular configuration without requiring synthesis and insertion of a completely new membrane molecule. It is suggested that the surface galactosyltransferase might function to repair damage to syncytial trophoblast glycocalyx induced by enzymes in maternal blood.

Original languageEnglish
Pages (from-to)267-281
Number of pages15
JournalGynecologic Investigation
Issue number5-6
StatePublished - Jan 1 1977

Fingerprint Dive into the research topics of 'Galactosyltransferase activity of the microvillous surface of human placental syncytial trophoblast'. Together they form a unique fingerprint.

  • Cite this