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- Publisher
- Wiley
- Copyright
- Copyright © 1993 Wiley Subscription Services, Inc., A Wiley Company
- ISSN
- 0730-2312
- eISSN
- 1097-4644
- DOI
- 10.1002/jcb.240520304
- pmid
- 7690043
- Publisher site
- See Article on Publisher Site
Abstract
β1,4 galactosyl‐ and α2,6 sialyltransferase (gal‐T EC 2.4.1.22 and sialyl‐T EC 2.4.99.1) sequentially elongate and terminate complex N‐glycan chains of glycoproteins. Both enzymes reside in trans Golgi cisternae; their ultrastructural relationship, however, is unknown. To delineate their respective Golgi compartment(s) we conducted a double label immunofluorescent study by conventional and confocal laser scanning microscopy in HepG2, HeLa, and other cells in presence of Golgi‐disturbing agents. Polyclonal, peptide‐specific antibodies to human sialyl‐T expressed as a β‐galactosidase‐sialyl‐T fusion protein in E. coli were developed and applied together with mABs to human milk gal‐T.
Journal
Journal of Cellular Biochemistry – Wiley
Published: Jul 1, 1993
Keywords: ; ; ; ; ;