Two yeast peroxisomal proteins crossreact with an antiserum against human sterol carrier protein 2 (SCP-2).
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.
Institut für Biochemie und Lebensmittelchemie, Technische Universität Graz, Austria.
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Tahotna
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Hapala
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Zinser
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Flekl
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Paltauf
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Daum
D000937:Antigen-Antibody Reactions; D002352:Carrier Proteins / Q000276:immunology*; D003429:Cross Reactions; D005656:Fungal Proteins / Q000276:immunology*; D006801:Humans; D007106:Immune Sera / Q000276:immunology*; D008830:Microbodies / Q000737:chemistry / Q000648:ultrastructure; D012441:Saccharomyces cerevisiae / Q000737:chemistry; D013261:Sterols; D013347:Subcellular Fractions / Q000737:chemistry
D002352:Carrier Proteins; D005656:Fungal Proteins; D007106:Immune Sera; D013261:Sterols