Immunologic relatedness of extracellular ligninases from the actinomycetesstreptomyces viridosporus t7a andstreptomyces badius 252 |
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Authors: | Magnuson Timothy S Roberts Mark A Crawford Don L Hertel Greg |
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Institution: | 1.Department of Bacteriology and Biochemistry, Institute for Molecular and Agricultural Genetic Engineering (IMAGE), University of Idaho, 83843, Moscow, ID ; |
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Abstract: | Four isoforms of the extracellular lignin peroxidase of the ligninolytic actinomyceteStreptomyces viridosporus T7A (ALip-P1, P2, P3, and P4) were individually purified by ultrafiltration and ammonium sulfate precipitation, followed
by electro-elution using polyacrylamide gel electrophoresis. Three of the purified peroxidases were compared for their immunologic
relatedness by Western blot analysis using a polyclonal antibody preparation produced in rabbits against pure isoform P3.
The anti-P3 antibody was also tested for its reactivity towards a lignin peroxidase from the white-rot fungusPhanerochaete chrysosporium and another ligninolytic actinomyceteStreptomyces badius 252. Results showed that peroxidases ALip-P1 through ALip-P3 are immunologically related to one another. The peroxidases
ofS. badius, but not the peroxidase ofP. chrysosporium, also reacted with the antibody, thus indicating that the lignin peroxidases ofS. viridosporus andS. badius are immunologically related. Based upon its specific affinity, lignin peroxidase isoform ALip-P3 ofS. viridosporus was readily purified using an anti-P3 antibody affinity column. |
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Keywords: | Index Entries" target="_blank">Index Entries Ligninases Western blot analysis affinity purification |
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