Purification and characterization of an aminopeptidase from the fungusSaccobolus platensis

A major aminopeptidase was purified to apparent homogeneity from soluble extracts of the fungusSaccobolus platensis by DEAE-cellulose, phenyl-Sepharose, Sephacryl S-300 chromatography, and disc polyacrylamide gel electrophoresis. Peptidase activity was measured with the radioactive peptide substrate...

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Detalles Bibliográficos
Autores principales:	Murray, P.F., Samela, A., Passeron, S.
Formato:	JOUR
Materias:	ascomycetes peptidase peptide processing phosphopeptide
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_01475975_v16_n4_p279_Murray
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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