Literature DB >> 6145409

Cell-free translation of messenger RNA for human bisphosphoglyceromutase.

A Dubart, P H Romeo, A Tsapis, M Goossens, R Rosa, J Rosa.   

Abstract

mRNAs prepared from different human tissues were translated in a cell-free reticulocyte lysate system and, when present, the neosynthesized bisphosphoglyceromutase ( BPGM ) was specifically isolated by immunoprecipitation and analyzed by polyacrylamide gel electrophoresis. Analysis of the translation products showed that bisphosphoglyceromutase was synthesized in vitro with its mature molecular weight and messenger RNA specifying the synthesis of BPGM exhibited a sedimentation coefficient of 12 S in human reticulocytes. This synthesis seems to be highly tissue specific since we could not evidence any synthesis of this enzyme using mRNA obtained from non erythroid tissue. The BPGM synthesis represents 0.1% of the total neosynthesized non heme proteins in human reticulocyte and ten times less (0.01%) in human fetal liver.

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Year:  1984        PMID: 6145409     DOI: 10.1016/0006-291x(84)91273-7

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  A recombinant bisphosphoglycerate mutase variant with acid phosphatase homology degrades 2,3-diphosphoglycerate.

Authors:  M C Garel; N Arous; M C Calvin; C T Craescu; J Rosa; R Rosa
Journal:  Proc Natl Acad Sci U S A       Date:  1994-04-26       Impact factor: 11.205

2.  Molecular cloning and sequencing of the human erythrocyte 2,3-bisphosphoglycerate mutase cDNA: revised amino acid sequence.

Authors:  V Joulin; J Peduzzi; P H Roméo; R Rosa; C Valentin; A Dubart; B Lapeyre; Y Blouquit; M C Garel; M Goossens
Journal:  EMBO J       Date:  1986-09       Impact factor: 11.598

  2 in total

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