Post-translational polymorphism of human IgA identified by immunoisoelectrofocusing

G De Benedictis; G Rose; C Brancati

doi:10.1111/j.1744-313x.1990.tb00858.x

Post-translational polymorphism of human IgA identified by immunoisoelectrofocusing

J Immunogenet. 1990 Feb-Apr;17(1-2):43-50. doi: 10.1111/j.1744-313x.1990.tb00858.x.

Authors

G De Benedictis¹, G Rose, C Brancati

Affiliation

¹ Department of Cell Biology, University of Calabria, Arcavacata, CS, Italy.

PMID: 2212700
DOI: 10.1111/j.1744-313x.1990.tb00858.x

Abstract

Immunoisoelectrofocusing (IIEF) reveals a microheterogeneity of human serum IgA controlled by an autosomal polymorphic gene, termed S. The microheterogeneity disappears when sialic acid is removed from serum glycoproteins by neuraminidase treatment. It can be postulated, therefore, that S encodes a sialyltransferase which attaches sialic acid at the outer prosthetic chains of IgA.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Humans
Immunoglobulin A / genetics*
Immunoglobulin A / isolation & purification
Immunoglobulin A / metabolism
Isoelectric Focusing
Phenotype
Polymorphism, Genetic
Protein Processing, Post-Translational / genetics
Sialyltransferases / genetics
beta-D-Galactoside alpha 2-6-Sialyltransferase

Substances

Immunoglobulin A
Sialyltransferases
beta-D-Galactoside alpha 2-6-Sialyltransferase