Literature DB >> 3802547

Purification of porphobilinogen deaminase from human erythrocytes by fast protein liquid chromatography.

F W de Rooij, C M Hamer, J H Wilson.   

Abstract

A four-step procedure using fast protein liquid chromatography is described for the isolation of porphobilinogen deaminase from human erythrocytes. The specific activity of the porphobilinogen deaminase is increased about 13,000-fold, and the preparation is electrophoretically pure on SDS-polyacrylamide gel electrophoresis.

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Year:  1987        PMID： 3802547     DOI： 10.1016/0009-8981(87)90233-6

Source DB:  PubMed          Journal:  Clin Chim Acta        ISSN： 0009-8981            Impact factor:   3.786


  3 in total

1.  A point mutation G----A in exon 12 of the porphobilinogen deaminase gene results in exon skipping and is responsible for acute intermittent porphyria.

Authors:  B Grandchamp; C Picat; F de Rooij; C Beaumont; P Wilson; J C Deybach; Y Nordmann
Journal:  Nucleic Acids Res       Date:  1989-08-25       Impact factor: 16.971

2.  Two different point G to A mutations in exon 10 of the porphobilinogen deaminase gene are responsible for acute intermittent porphyria.

Authors:  M H Delfau; C Picat; F W de Rooij; K Hamer; M Bogard; J H Wilson; J C Deybach; Y Nordmann; B Grandchamp
Journal:  J Clin Invest       Date:  1990-11       Impact factor: 14.808

3.  A simple rapid purification scheme for hydroxymethylbilane synthase from human erythrocytes.

Authors:  E Smythe; D C Williams
Journal:  Biochem J       Date:  1988-04-01       Impact factor: 3.857
  3 in total

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