Affiliation:
1. Lehrstuhl für Physiologie und Biochemie der Pflanzen, Universität Konstanz, D-7750 Konstanz, Bundesrepublik Deutschland
Abstract
Abstract
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 determinants 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.
Subject
General Biochemistry, Genetics and Molecular Biology
Cited by
6 articles.
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