Cyclic nucleotide phosphodiesterase activity in Neurospora crassa Purification by immunoaffinity chromatography and characterization

Monoclonal antibodies to Neurospora crassa cyclic nucleotide phosphodiesterase (PDE I) were selected by their capacity to inhibit the enzyme activity. The monoclonal immunoglobulin, coupled to Sepharose 4B, was used for the affinity purification of PDE I activity. After SDS-polyacrylamide gel electr...

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Autores principales: Rubinstein, Clara Patricia, Molina y Vedia, Luis Miguel, Torres, Héctor Norberto
Publicado: 1988
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Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v241_n1-2_p219_Ulloa
http://hdl.handle.net/20.500.12110/paper_00145793_v241_n1-2_p219_Ulloa
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Sumario:Monoclonal antibodies to Neurospora crassa cyclic nucleotide phosphodiesterase (PDE I) were selected by their capacity to inhibit the enzyme activity. The monoclonal immunoglobulin, coupled to Sepharose 4B, was used for the affinity purification of PDE I activity. After SDS-polyacrylamide gel electrophoresis the affinity purified PDE I fractions showed a single polypeptide band of about 41 kDa. This band reacted in Western blots with the above mentioned monoclonal immunoglobulin. © 1988.