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

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Standard

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

I: EMBO Journal, Bind 6, Nr. 10, 1987, s. 2891-6.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Danielsen, EM 1987, 'Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte', EMBO Journal, bind 6, nr. 10, s. 2891-6.

APA

Danielsen, E. M. (1987). Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte. EMBO Journal, 6(10), 2891-6.

Vancouver

Danielsen EM. Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte. EMBO Journal. 1987;6(10):2891-6.

Author

Danielsen, E M. / Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte. I: EMBO Journal. 1987 ; Bind 6, Nr. 10. s. 2891-6.

Bibtex

@article{e81b3cf0e7bc11ddbf70000ea68e967b,
title = "Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte",
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.",
author = "Danielsen, {E M}",
note = "Keywords: Alkaloids; Aminopeptidases; Animals; Glucan 1,4-alpha-Glucosidase; Glucosidases; Glycoside Hydrolases; Indolizines; Intestinal Mucosa; Intestine, Small; Microvilli; Multienzyme Complexes; Organ Culture Techniques; Protein Processing, Post-Translational; Sucrase-Isomaltase Complex; Sulfur Radioisotopes; Swainsonine; Swine; Tyrosine",
year = "1987",
language = "English",
volume = "6",
pages = "2891--6",
journal = "E M B O Journal",
issn = "0261-4189",
publisher = "Wiley-Blackwell",
number = "10",

}

RIS

TY - JOUR

T1 - Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte

AU - Danielsen, E M

N1 - Keywords: Alkaloids; Aminopeptidases; Animals; Glucan 1,4-alpha-Glucosidase; Glucosidases; Glycoside Hydrolases; Indolizines; Intestinal Mucosa; Intestine, Small; Microvilli; Multienzyme Complexes; Organ Culture Techniques; Protein Processing, Post-Translational; Sucrase-Isomaltase Complex; Sulfur Radioisotopes; Swainsonine; Swine; Tyrosine

PY - 1987

Y1 - 1987

N2 - 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.

AB - 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.

M3 - Journal article

C2 - 3121301

VL - 6

SP - 2891

EP - 2896

JO - E M B O Journal

JF - E M B O Journal

SN - 0261-4189

IS - 10

ER -

ID: 9881129