N-glycosylation site occupancy of rat alpha-1,3-fucosyltransferase IV and the effect of glycosylation on enzymatic activity.

doi:10.1016/s0304-4165(00)00094-5

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Article

N-glycosylation site occupancy of rat alpha-1,3-fucosyltransferase IV and the effect of glycosylation on enzymatic activity.

Biochimica et biophysica acta - 26 Jul 2000

Baboval T, Koul O, Smith F I

Abstract excerpt

All mammalian alpha-1,3-fucosyltransferases (Fuc-Ts) so far characterized have potential N-glycosylation sites, but the role of these sites in enzymatic activity or localization has not been investigated. When one member of this family, rFuc-TIV, is expressed in bacteria, the unglycosylated form of rFuc-TIV has no detectable enzymatic activity. The two potential N-glycosylation sites of rFuc-TIV were mutated to...

Topics

Animals
Binding Sites
Blotting, Western
COS Cells
Fucosyltransferases
Glycosylation
Golgi Apparatus
Immunohistochemistry
Isoelectric Focusing
Isopropyl Thiogalactoside
Mutagenesis, Site-Directed
Mutation
Plasmids
Rats
Transfection

Source

Open in PubMed

Identifiers

PMID: 10913840
DOI: 10.1016/s0304-4165(00)00094-5

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