Literature DB >> 6625164

Use of benzyldimethyl-n-hexadecylammonium chloride ("16-BAC"), a cationic detergent, in an acidic polyacrylamide gel electrophoresis system to detect base labile protein methylation in intact cells.

D E Macfarlane.   

Abstract

A discontinuous polyacrylamide gel system operating at pH 4.0-1.5 which resolves proteins bearing base labile groups extracted from intact cells is described. It uses potassium phosphate buffer in the running and stacking gel and glycine as the trailing ion component. Proteins are solubilized with urea and benzyldimethyl-n-hexadecylammonium chloride, a cationic detergent. The utility of the system is illustrated by fluorographs of the pattern of protein methylation in blood platelets and the HL60 promyelocyte cell line.

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Year:  1983        PMID: 6625164     DOI: 10.1016/0003-2697(83)90001-5

Source DB:  PubMed          Journal:  Anal Biochem        ISSN: 0003-2697            Impact factor:   3.365


  3 in total

1.  Asymmetrical distribution of L-isoaspartyl protein carboxyl methyltransferases in the plasma membranes of rat kidney cortex.

Authors:  D Gingras; D Boivin; R Beliveau
Journal:  Biochem J       Date:  1994-01-01       Impact factor: 3.857

2.  Spontaneous methylation of hemoglobin by S-adenosyl-methionine by a specific and saturable mechanism.

Authors:  A L Kimzey; P N McFadden
Journal:  J Protein Chem       Date:  1994-08

3.  Depletion of arachidonic acid from GH3 cells. Effects on inositol phospholipid turnover and cellular activation.

Authors:  D T Dudley; D E Macfarlane; A A Spector
Journal:  Biochem J       Date:  1987-09-15       Impact factor: 3.857

  3 in total

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