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.
Tahotna
D
D
Institut für Biochemie und Lebensmittelchemie, Technische Universität Graz, Austria.
Hapala
I
I
Zinser
E
E
Flekl
W
W
Paltauf
F
F
Daum
G
G
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