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
Autor principal: Samela, Andrea Silvia
Publicado: 1992
Materias:
ascomycetes
peptidase
peptide processing
phosphopeptide
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01475975_v16_n4_p279_Murray
http://hdl.handle.net/20.500.12110/paper_01475975_v16_n4_p279_Murray
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_01475975_v16_n4_p279_Murray
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spelling paper:paper_01475975_v16_n4_p279_Murray2023-06-08T15:12:45Z Purification and characterization of an aminopeptidase from the fungusSaccobolus platensis Samela, Andrea Silvia ascomycetes peptidase peptide processing phosphopeptide 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 Leu-Arg-Arg-Ala-Ser[32P]-Leu-Gly. The purified enzyme was a monomeric protein with a molecular mass of 90 kDa. The optimun pH of the enzyme activity was in the range 7.4-7.6. It was inhibited remarkably by EDTA, 1,10-phenanthroline, puromycin, amastatin, bestatin, and hydrophobic amino acids. The enzyme had a low substrate specificity and a requirement for free α-amino groups. Saccobolus peptidase had no measurable endoproteolytic activity and the exoproteolytic activity was evidenced on small peptides, suggesting that it might be involved in the late stage of protein turnover events. © 1992 Academic Press, Inc. Fil:Samela, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1992 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01475975_v16_n4_p279_Murray http://hdl.handle.net/20.500.12110/paper_01475975_v16_n4_p279_Murray
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic ascomycetes
peptidase
peptide processing
phosphopeptide
spellingShingle ascomycetes
peptidase
peptide processing
phosphopeptide
Samela, Andrea Silvia
Purification and characterization of an aminopeptidase from the fungusSaccobolus platensis
topic_facet ascomycetes
peptidase
peptide processing
phosphopeptide
description 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 Leu-Arg-Arg-Ala-Ser[32P]-Leu-Gly. The purified enzyme was a monomeric protein with a molecular mass of 90 kDa. The optimun pH of the enzyme activity was in the range 7.4-7.6. It was inhibited remarkably by EDTA, 1,10-phenanthroline, puromycin, amastatin, bestatin, and hydrophobic amino acids. The enzyme had a low substrate specificity and a requirement for free α-amino groups. Saccobolus peptidase had no measurable endoproteolytic activity and the exoproteolytic activity was evidenced on small peptides, suggesting that it might be involved in the late stage of protein turnover events. © 1992 Academic Press, Inc.
author Samela, Andrea Silvia
author_facet Samela, Andrea Silvia
author_sort Samela, Andrea Silvia
title Purification and characterization of an aminopeptidase from the fungusSaccobolus platensis
title_short Purification and characterization of an aminopeptidase from the fungusSaccobolus platensis
title_full Purification and characterization of an aminopeptidase from the fungusSaccobolus platensis
title_fullStr Purification and characterization of an aminopeptidase from the fungusSaccobolus platensis
title_full_unstemmed Purification and characterization of an aminopeptidase from the fungusSaccobolus platensis
title_sort purification and characterization of an aminopeptidase from the fungussaccobolus platensis
publishDate 1992
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01475975_v16_n4_p279_Murray
http://hdl.handle.net/20.500.12110/paper_01475975_v16_n4_p279_Murray
work_keys_str_mv AT samelaandreasilvia purificationandcharacterizationofanaminopeptidasefromthefungussaccobolusplatensis
_version_ 1768546341674287104

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