Literature DB >> 3681952

Laterobasal membranes from intestinal epithelial cells: isolation free of intracellular membrane contaminants.

T D Nguyen1, J P Broyart, K T Ngu, A Illescas, A K Mircheff, G M Gray.   

Abstract

A simplified method for isolating highly purified laterobasal membranes (LBM) from enterocytes is based on treatment of membranes with 8 mM CaCl2 concentration in order to aggregate intracellular membrane contaminants. The resultant LBM showed an average 15-fold enrichment and constituted 8% of the original K-stimulated phosphatase in the initial crude homogenate. It showed typical LBM migration on counter-current distribution (CCD) and was essentially free of contamination with endoplasmic reticulum and Golgi membranes. This method is highly efficient and yields sufficient purified LBM to allow comprehensive analysis of enterocyte membrane events.

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Year:  1987        PMID: 3681952     DOI: 10.1007/bf01871183

Source DB:  PubMed          Journal:  J Membr Biol        ISSN: 0022-2631            Impact factor:   1.843


  19 in total

1.  The surface membrane of the small intestinal epithelial cell. I. Localization of adenyl cyclase.

Authors:  H Murer; E Ammann; J Biber; U Hopfer
Journal:  Biochim Biophys Acta       Date:  1976-05-21

2.  Analytical isolation of plasma membranes of intestinal epithelial cells: identification of Na, K-ATPase rich membranes and the distribution of enzyme activities.

Authors:  A K Mircheff; E M Wright
Journal:  J Membr Biol       Date:  1976-09-17       Impact factor: 1.843

3.  The digestive function of the epithelium of the small intestine. II. Localization of disaccharide hydrolysis in the isolated brush border portion of intestinal epithelial cells.

Authors:  D MILLER; R K CRANE
Journal:  Biochim Biophys Acta       Date:  1961-09-16

4.  Complex subcellular distributions of enzymatic markers in intestinal epithelial cells.

Authors:  A K Mircheff; D J Ahnen; A Islam; N A Santiago; G M Gray
Journal:  J Membr Biol       Date:  1985       Impact factor: 1.843

5.  Intestinal surface aminooligopeptidase. Distinct molecular forms during assembly on intracellular membranes in vivo.

Authors:  D J Ahnen; A K Mircheff; N A Santiago; C Yoshioka; G M Gray
Journal:  J Biol Chem       Date:  1983-05-10       Impact factor: 5.157

6.  Arylesterase in serum: elaboration and clinical application of a fixed-incubation method.

Authors:  K Lorentz; B Flatter; E Augustin
Journal:  Clin Chem       Date:  1979-10       Impact factor: 8.327

7.  Incomplete intracellular forms of intestinal surface membrane sucrase-isomaltase.

Authors:  J P Cezard; K A Conklin; B C Das; G M Gray
Journal:  J Biol Chem       Date:  1979-09-25       Impact factor: 5.157

8.  Synthesis of membrane glycoproteins in rat small-intestinal villus cells. Redistribution of L-[1,5,6-3H]fucose-labelled membrane glycoproteins among Golgi, lateral basal and microvillus membranes in vivo.

Authors:  A Quaroni; K Kirsch; M M Weiser
Journal:  Biochem J       Date:  1979-07-15       Impact factor: 3.857

9.  Immunocytochemical demonstration of ecto-galactosyltransferase in absorptive intestinal cells.

Authors:  J Roth; M J Lentze; E G Berger
Journal:  J Cell Biol       Date:  1985-01       Impact factor: 10.539

10.  Synthesis of plasmalemmal glycoproteins in intestinal epithelial cells. Separation of Golgi membranes from villus and crypt cell surface membranes; glycosyltransferase activity of surface membrane.

Authors:  M M Weiser; M M Neumeier; A Quaroni; K Kirsch
Journal:  J Cell Biol       Date:  1978-06       Impact factor: 10.539

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  2 in total

1.  Glycyl-L-proline transport in rabbit enterocyte basolateral-membrane vesicles.

Authors:  J Dyer; R B Beechey; J P Gorvel; R T Smith; R Wootton; S P Shirazi-Beechey
Journal:  Biochem J       Date:  1990-08-01       Impact factor: 3.857

2.  Sucrase-alpha-dextrinase in the rat. Postinsertional conversion to inactive molecular species by a carbohydrate-free diet.

Authors:  R Quan; G M Gray
Journal:  J Clin Invest       Date:  1993-06       Impact factor: 14.808

  2 in total

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