Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
EMBO J. 1987 Oct;6(10):2891-6.

Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte.

Author information

  • Department of Biochemistry C, Panum Institute, University of Copenhagen, Denmark.

Abstract

Protein sulfation in small intestinal epithelial cells was studied by labelling of organ cultured mucosal explants with [35S]-sulfate. Six bands in SDS-PAGE became selectively labelled; four, of 250, 200, 166 and 130 kd, were membrane-bound and two, of 75 and 60 kd, were soluble. The sulfated membrane-bound components were all enriched in the microvillar fraction but either absent or barely detectable in intracellular or basolateral membranes. Immunopurification of sucrase-isomaltase, maltase-glucoamylase, aminopeptidase N and aminopeptidase A showed that these microvillar enzymes become sulfated. Most if not all the sulfate was bound to tyrosine residues rather than to the carbohydrate of the microvillar enzymes, showing that this type of modification can occur on plasma membrane proteins as well as on secretory proteins.

PMID:
3121301
[PubMed - indexed for MEDLINE]
PMCID:
PMC553723
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for PubMed Central
    Loading ...
    Write to the Help Desk