Literature DB >> 8499465

Two yeast peroxisomal proteins crossreact with an antiserum against human sterol carrier protein 2 (SCP-2).

D Tahotna1, I Hapala, E Zinser, W Flekl, F Paltauf, G Daum.   

Abstract

An antibody raised against human sterol carrier protein 2 (SCP-2) crossreacts with two yeast peroxisomal proteins. These proteins have apparent molecular weights of 35 and 58 kDa. Subfractionation of peroxisomes revealed that the 58 kDa species is a soluble matrix protein, whereas the 35 kDa protein is membrane bound. Treatment of isolated peroxisomal membranes with 0.25 M KCl released the 35 kDa crossreactive protein into the soluble supernatant. However, lipid transfer activity could be attributed neither to the 35 kDa nor to the 58 kDa protein.

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Year:  1993        PMID: 8499465     DOI: 10.1016/0005-2736(93)90175-y

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

Review 1.  Acyl-CoA binding proteins: multiplicity and function.

Authors:  R E Gossett; A A Frolov; J B Roths; W D Behnke; A B Kier; F Schroeder
Journal:  Lipids       Date:  1996-09       Impact factor: 1.880

2.  Transcriptional regulation of phospholipid biosynthesis is linked to fatty acid metabolism by an acyl-CoA-binding-protein-dependent mechanism in Saccharomyces cerevisiae.

Authors:  Søren Feddersen; Thomas B F Neergaard; Jens Knudsen; Nils J Faergeman
Journal:  Biochem J       Date:  2007-10-15       Impact factor: 3.857

  2 in total

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