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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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
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_01475975_v16_n4_p279_Murray
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spelling todo:paper_01475975_v16_n4_p279_Murray2023-10-03T15:00:32Z Purification and characterization of an aminopeptidase from the fungusSaccobolus platensis Murray, P.F. Samela, A. Passeron, S. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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
Murray, P.F.
Samela, A.
Passeron, S.
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.
format JOUR
author Murray, P.F.
Samela, A.
Passeron, S.
author_facet Murray, P.F.
Samela, A.
Passeron, S.
author_sort Murray, P.F.
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
url http://hdl.handle.net/20.500.12110/paper_01475975_v16_n4_p279_Murray
work_keys_str_mv AT murraypf purificationandcharacterizationofanaminopeptidasefromthefungussaccobolusplatensis
AT samelaa purificationandcharacterizationofanaminopeptidasefromthefungussaccobolusplatensis
AT passerons purificationandcharacterizationofanaminopeptidasefromthefungussaccobolusplatensis
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