Literature DB >> 7380394

Purification of glyoxysomal acetyl-CoA acyltransferase.

J Frevert, H Kindl.   

Abstract

Acetyl-CoA acyltransferase was extracted from cotyledons of germinating cucumber seeds and purified to apparent heomogeneity. The purification based primarily on cation exchange chromatography and separation on an affinity gel. The enzyme is a dimer consisting of two subunits of molecular weight 45 000. Acetyl-CoA acyltransferase was localized in glyoxysomes, the matrix was found to be the site of thiolase function within the organelle.

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Year:  1980        PMID: 7380394     DOI: 10.1515/bchm2.1980.361.1.537

Source DB:  PubMed          Journal:  Hoppe Seylers Z Physiol Chem        ISSN: 0018-4888


  4 in total

1.  Phylogenetic analysis of the thiolase family. Implications for the evolutionary origin of peroxisomes.

Authors:  J C Igual; C González-Bosch; J Dopazo; J E Pérez-Ortín
Journal:  J Mol Evol       Date:  1992-08       Impact factor: 2.395

2.  Thiolase mRNA translated in vitro yields a peptide with a putative N-terminal presequence.

Authors:  R Preisig-Müller; H Kindl
Journal:  Plant Mol Biol       Date:  1993-04       Impact factor: 4.076

3.  Peroxisomal thiolase mRNA is induced during mango fruit ripening.

Authors:  G Bojorquez; M A Gómez-Lim
Journal:  Plant Mol Biol       Date:  1995-08       Impact factor: 4.076

4.  Cloning, expression and purification of an acetoacetyl CoA thiolase from sunflower cotyledon.

Authors:  James H Dyer; Anthony Maina; Iris D Gomez; Melissa Cadet; Silke Oeljeklaus; Anke C Schiedel
Journal:  Int J Biol Sci       Date:  2009-12-02       Impact factor: 6.580

  4 in total

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