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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todo:paper_01475975_v19_n3_p214_Murray2023-10-03T15:00:33Z The Soluble Aminopeptidase System from Saccobolus platensis. Characterization of a New Glutamate Aminopeptidase Murray, P.F. Passeron, S. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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 Murray, P.F. Passeron, S. 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. |
| format |
JOUR |
| author |
Murray, P.F. Passeron, S. |
| author_facet |
Murray, P.F. Passeron, S. |
| author_sort |
Murray, P.F. |
| 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 |
| url |
http://hdl.handle.net/20.500.12110/paper_01475975_v19_n3_p214_Murray |
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1807318531281256448 |