Antiserum Against the 33-kDa Herbicide-Binding Protein
نویسندگان
چکیده
Gerhard Herrmann, Andreas Thiel, and Peter Böger Lehrstuhl für Physiologie und Biochemie der Pflanzen, Universität Konstanz, D-7750 Konstanz, Bundesrepublik Deutschland Z. Naturforsch. 40c, 814—818 (1985); received August 9, 1985 Photosystem-II Particles, Immunoblotting, Antibody Agglutination, Cross Reaction, Urea-Gradient Gel Electrophoresis A rabbit antiserum was prepared against the purified 33-kDa herbicide-binding protein (HBP) from the alga Bumilleriopsis filiformis. Specificity at 1:10,000 dilution (v/v) of the unpurified serum is detectable in the immunoblotting assay with both the 33-kDa protein from the alga Bumilleriopsis as well as that from Spinacia. Agglutination can be observed with photosystem-II particles only, not with intact thylakoids, indicative of a hidden location of the protein determi nants in the membrane. Neither herbicide binding nor electron transport is influenced by the antibody. Apparently, the antigenic site of the HBP for the antibody used here is different from the herbicide-binding region.
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