The Soluble Aminopeptidase System from Saccobolus platensis. Characterization of a New Glutamate Aminopeptidase

Fernández, Murray, P., and Passeron, S. 1995. The soluble aminopeptidase system from Saccobolus platensis. Characterization of a new glutamate aminopeptidase. Experimental Mycology 19, 214-222. The aminopeptidase pattern from the fungus Saccobolus platensis was investigated by ion-exchange chromatog...

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Publicado:	1995
Materias:	aminopeptidase peptide degradation proteolysis bestatin fungal protein glutamic acid glutamyl aminopeptidase microsomal aminopeptidase phenanthroline proline aminopeptidase unclassified drug article controlled study enzyme activity enzyme inhibition enzyme isolation enzyme purification enzyme substrate fungus ion exchange chromatography molecular weight nonhuman pH priority journal saccobolus platensis Fungi Saccobolus
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01475975_v19_n3_p214_Murray http://hdl.handle.net/20.500.12110/paper_01475975_v19_n3_p214_Murray
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_01475975_v19_n3_p214_Murray
record_format	dspace
spelling	paper:paper_01475975_v19_n3_p214_Murray2023-06-08T15:12:46Z The Soluble Aminopeptidase System from Saccobolus platensis. Characterization of a New Glutamate Aminopeptidase aminopeptidase peptide degradation proteolysis aminopeptidase bestatin fungal protein glutamic acid glutamyl aminopeptidase microsomal aminopeptidase phenanthroline proline aminopeptidase unclassified drug article controlled study enzyme activity enzyme inhibition enzyme isolation enzyme purification enzyme substrate fungus ion exchange chromatography molecular weight nonhuman pH priority journal saccobolus platensis Fungi Saccobolus Fernández, Murray, P., and Passeron, S. 1995. The soluble aminopeptidase system from Saccobolus platensis. Characterization of a new glutamate aminopeptidase. Experimental Mycology 19, 214-222. The aminopeptidase pattern from the fungus Saccobolus platensis was investigated by ion-exchange chromatography fractionation of the soluble proteins. The chromogenic p-nitroanilide derivatives of nine different amino acids were used as substrates. Apart from the previously characterized major alanine aminopeptidase (P. Fernádez Murray, A. Samela, and S. Passeron, 1992. Exp. Mycol. 16, 279-290), two new minor aminopeptidase activities were found: one mainly a proline aminopeptidase and a second highly specific for the hydrolysis of the chromogenic derivative of glutamate. This last activity was subjected to ammonium sulfate fractionation and successive phenyl-Sepharose, DEAE-Sephacel, and Sephacryl S-200 HR column chromatography. A highly purified enzyme fraction was obtained. This new glutamate aminopeptidase had a molecular weight of 22 kDa and an optimum pH range of 7.2-8.0 and was inhibited by o-phenanthroline and bestatin. © 1995 Academic Press. All rights reserved. 1995 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01475975_v19_n3_p214_Murray http://hdl.handle.net/20.500.12110/paper_01475975_v19_n3_p214_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	aminopeptidase peptide degradation proteolysis aminopeptidase bestatin fungal protein glutamic acid glutamyl aminopeptidase microsomal aminopeptidase phenanthroline proline aminopeptidase unclassified drug article controlled study enzyme activity enzyme inhibition enzyme isolation enzyme purification enzyme substrate fungus ion exchange chromatography molecular weight nonhuman pH priority journal saccobolus platensis Fungi Saccobolus
spellingShingle	aminopeptidase peptide degradation proteolysis aminopeptidase bestatin fungal protein glutamic acid glutamyl aminopeptidase microsomal aminopeptidase phenanthroline proline aminopeptidase unclassified drug article controlled study enzyme activity enzyme inhibition enzyme isolation enzyme purification enzyme substrate fungus ion exchange chromatography molecular weight nonhuman pH priority journal saccobolus platensis Fungi Saccobolus The Soluble Aminopeptidase System from Saccobolus platensis. Characterization of a New Glutamate Aminopeptidase
topic_facet	aminopeptidase peptide degradation proteolysis aminopeptidase bestatin fungal protein glutamic acid glutamyl aminopeptidase microsomal aminopeptidase phenanthroline proline aminopeptidase unclassified drug article controlled study enzyme activity enzyme inhibition enzyme isolation enzyme purification enzyme substrate fungus ion exchange chromatography molecular weight nonhuman pH priority journal saccobolus platensis Fungi Saccobolus
description	Fernández, Murray, P., and Passeron, S. 1995. The soluble aminopeptidase system from Saccobolus platensis. Characterization of a new glutamate aminopeptidase. Experimental Mycology 19, 214-222. The aminopeptidase pattern from the fungus Saccobolus platensis was investigated by ion-exchange chromatography fractionation of the soluble proteins. The chromogenic p-nitroanilide derivatives of nine different amino acids were used as substrates. Apart from the previously characterized major alanine aminopeptidase (P. Fernádez Murray, A. Samela, and S. Passeron, 1992. Exp. Mycol. 16, 279-290), two new minor aminopeptidase activities were found: one mainly a proline aminopeptidase and a second highly specific for the hydrolysis of the chromogenic derivative of glutamate. This last activity was subjected to ammonium sulfate fractionation and successive phenyl-Sepharose, DEAE-Sephacel, and Sephacryl S-200 HR column chromatography. A highly purified enzyme fraction was obtained. This new glutamate aminopeptidase had a molecular weight of 22 kDa and an optimum pH range of 7.2-8.0 and was inhibited by o-phenanthroline and bestatin. © 1995 Academic Press. All rights reserved.
title	The Soluble Aminopeptidase System from Saccobolus platensis. Characterization of a New Glutamate Aminopeptidase
title_short	The Soluble Aminopeptidase System from Saccobolus platensis. Characterization of a New Glutamate Aminopeptidase
title_full	The Soluble Aminopeptidase System from Saccobolus platensis. Characterization of a New Glutamate Aminopeptidase
title_fullStr	The Soluble Aminopeptidase System from Saccobolus platensis. Characterization of a New Glutamate Aminopeptidase
title_full_unstemmed	The Soluble Aminopeptidase System from Saccobolus platensis. Characterization of a New Glutamate Aminopeptidase
title_sort	soluble aminopeptidase system from saccobolus platensis. characterization of a new glutamate aminopeptidase
publishDate	1995
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01475975_v19_n3_p214_Murray http://hdl.handle.net/20.500.12110/paper_01475975_v19_n3_p214_Murray
_version_	1768546670522400768

The Soluble Aminopeptidase System from Saccobolus platensis. Characterization of a New Glutamate Aminopeptidase

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