Characterization of an Aminopeptidase and a Proline Iminopeptidase from Cabbage Leaves

Aminopeptidase, preferring phenylalanine-p-nitroanilide as substrate, and proline iminopeptidase, highly-specific for proline-p-nitroanilide, were isolated from cabbage leaves (Brassica oleraceae var. capitata). As pH optima, 7.2−7.5 for aminopeptidase activity and 8.0−8.5 for proline iminopeptidase...
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Autor*in:	Marinova, Margarita [verfasserIn] Dolashki, Alexander Altenberend, Florian Stevanovic, Stefan Voelter, Wolfgang Tchorbanov, Bozhidar

Format:	Artikel

Erschienen:	2008

Anmerkung:	© 1946 – 2014: Verlag der Zeitschrift für Naturforschung

Übergeordnetes Werk:	Enthalten in: Zeitschrift für Naturforschung. C, Biosciences - Verlag der Zeitschrift für Naturforschung, 1973, 63(2008), 1-2 vom: 01. Feb., Seite 105-112
Übergeordnetes Werk:	volume:63 ; year:2008 ; number:1-2 ; day:01 ; month:02 ; pages:105-112

Links:	Volltext

DOI / URN:	10.1515/znc-2008-1-220

Katalog-ID:	OLC2138035662

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520			\|a Aminopeptidase, preferring phenylalanine-p-nitroanilide as substrate, and proline iminopeptidase, highly-specific for proline-p-nitroanilide, were isolated from cabbage leaves (Brassica oleraceae var. capitata). As pH optima, 7.2−7.5 for aminopeptidase activity and 8.0−8.5 for proline iminopeptidase were determined. Both peptidases were strongly inhibited by p-chloromercuribenzoic acid, heavy metal ions and urea. The molecular weights were determined by gel filtration to be 56 and 204 kDa, respectively. The iminopeptidase was decomposed during SDS electrophoresis to four subunits of 50 kDa. Minor impurities of myrosinase- associated protein (~70 kDa) were found in both preparations. Preliminary data of their amino acid sequences showed similarities to those of aminopeptidases N (family M1) and proline iminopeptidases (family S33).
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allfields	10.1515/znc-2008-1-220 doi (DE-627)OLC2138035662 (DE-B1597)znc-2008-1-220-p DE-627 ger DE-627 rakwb 500 VZ 570 VZ 12 ssgn BIODIV DE-30 fid Marinova, Margarita verfasserin aut Characterization of an Aminopeptidase and a Proline Iminopeptidase from Cabbage Leaves 2008 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © 1946 – 2014: Verlag der Zeitschrift für Naturforschung Aminopeptidase, preferring phenylalanine-p-nitroanilide as substrate, and proline iminopeptidase, highly-specific for proline-p-nitroanilide, were isolated from cabbage leaves (Brassica oleraceae var. capitata). As pH optima, 7.2−7.5 for aminopeptidase activity and 8.0−8.5 for proline iminopeptidase were determined. Both peptidases were strongly inhibited by p-chloromercuribenzoic acid, heavy metal ions and urea. The molecular weights were determined by gel filtration to be 56 and 204 kDa, respectively. The iminopeptidase was decomposed during SDS electrophoresis to four subunits of 50 kDa. Minor impurities of myrosinase- associated protein (~70 kDa) were found in both preparations. Preliminary data of their amino acid sequences showed similarities to those of aminopeptidases N (family M1) and proline iminopeptidases (family S33). Dolashki, Alexander aut Altenberend, Florian aut Stevanovic, Stefan aut Voelter, Wolfgang aut Tchorbanov, Bozhidar aut Enthalten in Zeitschrift für Naturforschung. C, Biosciences Verlag der Zeitschrift für Naturforschung, 1973 63(2008), 1-2 vom: 01. Feb., Seite 105-112 (DE-627)129307394 (DE-600)124636-7 (DE-576)014504936 0939-5075 nnns volume:63 year:2008 number:1-2 day:01 month:02 pages:105-112 https://doi.org/10.1515/znc-2008-1-220 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-FOR GBV_ILN_11 GBV_ILN_21 GBV_ILN_22 GBV_ILN_24 GBV_ILN_40 GBV_ILN_70 GBV_ILN_120 GBV_ILN_121 GBV_ILN_252 GBV_ILN_2001 GBV_ILN_2004 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2237 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4155 GBV_ILN_4219 GBV_ILN_4266 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4314 GBV_ILN_4320 AR 63 2008 1-2 01 02 105-112
spelling	10.1515/znc-2008-1-220 doi (DE-627)OLC2138035662 (DE-B1597)znc-2008-1-220-p DE-627 ger DE-627 rakwb 500 VZ 570 VZ 12 ssgn BIODIV DE-30 fid Marinova, Margarita verfasserin aut Characterization of an Aminopeptidase and a Proline Iminopeptidase from Cabbage Leaves 2008 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © 1946 – 2014: Verlag der Zeitschrift für Naturforschung Aminopeptidase, preferring phenylalanine-p-nitroanilide as substrate, and proline iminopeptidase, highly-specific for proline-p-nitroanilide, were isolated from cabbage leaves (Brassica oleraceae var. capitata). As pH optima, 7.2−7.5 for aminopeptidase activity and 8.0−8.5 for proline iminopeptidase were determined. Both peptidases were strongly inhibited by p-chloromercuribenzoic acid, heavy metal ions and urea. The molecular weights were determined by gel filtration to be 56 and 204 kDa, respectively. The iminopeptidase was decomposed during SDS electrophoresis to four subunits of 50 kDa. Minor impurities of myrosinase- associated protein (~70 kDa) were found in both preparations. Preliminary data of their amino acid sequences showed similarities to those of aminopeptidases N (family M1) and proline iminopeptidases (family S33). Dolashki, Alexander aut Altenberend, Florian aut Stevanovic, Stefan aut Voelter, Wolfgang aut Tchorbanov, Bozhidar aut Enthalten in Zeitschrift für Naturforschung. C, Biosciences Verlag der Zeitschrift für Naturforschung, 1973 63(2008), 1-2 vom: 01. Feb., Seite 105-112 (DE-627)129307394 (DE-600)124636-7 (DE-576)014504936 0939-5075 nnns volume:63 year:2008 number:1-2 day:01 month:02 pages:105-112 https://doi.org/10.1515/znc-2008-1-220 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-FOR GBV_ILN_11 GBV_ILN_21 GBV_ILN_22 GBV_ILN_24 GBV_ILN_40 GBV_ILN_70 GBV_ILN_120 GBV_ILN_121 GBV_ILN_252 GBV_ILN_2001 GBV_ILN_2004 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2237 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4155 GBV_ILN_4219 GBV_ILN_4266 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4314 GBV_ILN_4320 AR 63 2008 1-2 01 02 105-112
allfields_unstemmed	10.1515/znc-2008-1-220 doi (DE-627)OLC2138035662 (DE-B1597)znc-2008-1-220-p DE-627 ger DE-627 rakwb 500 VZ 570 VZ 12 ssgn BIODIV DE-30 fid Marinova, Margarita verfasserin aut Characterization of an Aminopeptidase and a Proline Iminopeptidase from Cabbage Leaves 2008 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © 1946 – 2014: Verlag der Zeitschrift für Naturforschung Aminopeptidase, preferring phenylalanine-p-nitroanilide as substrate, and proline iminopeptidase, highly-specific for proline-p-nitroanilide, were isolated from cabbage leaves (Brassica oleraceae var. capitata). As pH optima, 7.2−7.5 for aminopeptidase activity and 8.0−8.5 for proline iminopeptidase were determined. Both peptidases were strongly inhibited by p-chloromercuribenzoic acid, heavy metal ions and urea. The molecular weights were determined by gel filtration to be 56 and 204 kDa, respectively. The iminopeptidase was decomposed during SDS electrophoresis to four subunits of 50 kDa. Minor impurities of myrosinase- associated protein (~70 kDa) were found in both preparations. Preliminary data of their amino acid sequences showed similarities to those of aminopeptidases N (family M1) and proline iminopeptidases (family S33). Dolashki, Alexander aut Altenberend, Florian aut Stevanovic, Stefan aut Voelter, Wolfgang aut Tchorbanov, Bozhidar aut Enthalten in Zeitschrift für Naturforschung. C, Biosciences Verlag der Zeitschrift für Naturforschung, 1973 63(2008), 1-2 vom: 01. Feb., Seite 105-112 (DE-627)129307394 (DE-600)124636-7 (DE-576)014504936 0939-5075 nnns volume:63 year:2008 number:1-2 day:01 month:02 pages:105-112 https://doi.org/10.1515/znc-2008-1-220 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-FOR GBV_ILN_11 GBV_ILN_21 GBV_ILN_22 GBV_ILN_24 GBV_ILN_40 GBV_ILN_70 GBV_ILN_120 GBV_ILN_121 GBV_ILN_252 GBV_ILN_2001 GBV_ILN_2004 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2237 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4155 GBV_ILN_4219 GBV_ILN_4266 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4314 GBV_ILN_4320 AR 63 2008 1-2 01 02 105-112
allfieldsGer	10.1515/znc-2008-1-220 doi (DE-627)OLC2138035662 (DE-B1597)znc-2008-1-220-p DE-627 ger DE-627 rakwb 500 VZ 570 VZ 12 ssgn BIODIV DE-30 fid Marinova, Margarita verfasserin aut Characterization of an Aminopeptidase and a Proline Iminopeptidase from Cabbage Leaves 2008 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © 1946 – 2014: Verlag der Zeitschrift für Naturforschung Aminopeptidase, preferring phenylalanine-p-nitroanilide as substrate, and proline iminopeptidase, highly-specific for proline-p-nitroanilide, were isolated from cabbage leaves (Brassica oleraceae var. capitata). As pH optima, 7.2−7.5 for aminopeptidase activity and 8.0−8.5 for proline iminopeptidase were determined. Both peptidases were strongly inhibited by p-chloromercuribenzoic acid, heavy metal ions and urea. The molecular weights were determined by gel filtration to be 56 and 204 kDa, respectively. The iminopeptidase was decomposed during SDS electrophoresis to four subunits of 50 kDa. Minor impurities of myrosinase- associated protein (~70 kDa) were found in both preparations. Preliminary data of their amino acid sequences showed similarities to those of aminopeptidases N (family M1) and proline iminopeptidases (family S33). Dolashki, Alexander aut Altenberend, Florian aut Stevanovic, Stefan aut Voelter, Wolfgang aut Tchorbanov, Bozhidar aut Enthalten in Zeitschrift für Naturforschung. C, Biosciences Verlag der Zeitschrift für Naturforschung, 1973 63(2008), 1-2 vom: 01. Feb., Seite 105-112 (DE-627)129307394 (DE-600)124636-7 (DE-576)014504936 0939-5075 nnns volume:63 year:2008 number:1-2 day:01 month:02 pages:105-112 https://doi.org/10.1515/znc-2008-1-220 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-FOR GBV_ILN_11 GBV_ILN_21 GBV_ILN_22 GBV_ILN_24 GBV_ILN_40 GBV_ILN_70 GBV_ILN_120 GBV_ILN_121 GBV_ILN_252 GBV_ILN_2001 GBV_ILN_2004 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2237 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4155 GBV_ILN_4219 GBV_ILN_4266 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4314 GBV_ILN_4320 AR 63 2008 1-2 01 02 105-112
allfieldsSound	10.1515/znc-2008-1-220 doi (DE-627)OLC2138035662 (DE-B1597)znc-2008-1-220-p DE-627 ger DE-627 rakwb 500 VZ 570 VZ 12 ssgn BIODIV DE-30 fid Marinova, Margarita verfasserin aut Characterization of an Aminopeptidase and a Proline Iminopeptidase from Cabbage Leaves 2008 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © 1946 – 2014: Verlag der Zeitschrift für Naturforschung Aminopeptidase, preferring phenylalanine-p-nitroanilide as substrate, and proline iminopeptidase, highly-specific for proline-p-nitroanilide, were isolated from cabbage leaves (Brassica oleraceae var. capitata). As pH optima, 7.2−7.5 for aminopeptidase activity and 8.0−8.5 for proline iminopeptidase were determined. Both peptidases were strongly inhibited by p-chloromercuribenzoic acid, heavy metal ions and urea. The molecular weights were determined by gel filtration to be 56 and 204 kDa, respectively. The iminopeptidase was decomposed during SDS electrophoresis to four subunits of 50 kDa. Minor impurities of myrosinase- associated protein (~70 kDa) were found in both preparations. Preliminary data of their amino acid sequences showed similarities to those of aminopeptidases N (family M1) and proline iminopeptidases (family S33). Dolashki, Alexander aut Altenberend, Florian aut Stevanovic, Stefan aut Voelter, Wolfgang aut Tchorbanov, Bozhidar aut Enthalten in Zeitschrift für Naturforschung. C, Biosciences Verlag der Zeitschrift für Naturforschung, 1973 63(2008), 1-2 vom: 01. Feb., Seite 105-112 (DE-627)129307394 (DE-600)124636-7 (DE-576)014504936 0939-5075 nnns volume:63 year:2008 number:1-2 day:01 month:02 pages:105-112 https://doi.org/10.1515/znc-2008-1-220 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-FOR GBV_ILN_11 GBV_ILN_21 GBV_ILN_22 GBV_ILN_24 GBV_ILN_40 GBV_ILN_70 GBV_ILN_120 GBV_ILN_121 GBV_ILN_252 GBV_ILN_2001 GBV_ILN_2004 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2237 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4155 GBV_ILN_4219 GBV_ILN_4266 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4314 GBV_ILN_4320 AR 63 2008 1-2 01 02 105-112
source	Enthalten in Zeitschrift für Naturforschung. C, Biosciences 63(2008), 1-2 vom: 01. Feb., Seite 105-112 volume:63 year:2008 number:1-2 day:01 month:02 pages:105-112
sourceStr	Enthalten in Zeitschrift für Naturforschung. C, Biosciences 63(2008), 1-2 vom: 01. Feb., Seite 105-112 volume:63 year:2008 number:1-2 day:01 month:02 pages:105-112
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author	Marinova, Margarita
spellingShingle	Marinova, Margarita ddc 500 ddc 570 ssgn 12 fid BIODIV Characterization of an Aminopeptidase and a Proline Iminopeptidase from Cabbage Leaves
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topic_title	500 VZ 570 VZ 12 ssgn BIODIV DE-30 fid Characterization of an Aminopeptidase and a Proline Iminopeptidase from Cabbage Leaves
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title	Characterization of an Aminopeptidase and a Proline Iminopeptidase from Cabbage Leaves
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title_full	Characterization of an Aminopeptidase and a Proline Iminopeptidase from Cabbage Leaves
author_sort	Marinova, Margarita
journal	Zeitschrift für Naturforschung. C, Biosciences
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author_browse	Marinova, Margarita Dolashki, Alexander Altenberend, Florian Stevanovic, Stefan Voelter, Wolfgang Tchorbanov, Bozhidar
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title_sort	characterization of an aminopeptidase and a proline iminopeptidase from cabbage leaves
title_auth	Characterization of an Aminopeptidase and a Proline Iminopeptidase from Cabbage Leaves
abstract	Aminopeptidase, preferring phenylalanine-p-nitroanilide as substrate, and proline iminopeptidase, highly-specific for proline-p-nitroanilide, were isolated from cabbage leaves (Brassica oleraceae var. capitata). As pH optima, 7.2−7.5 for aminopeptidase activity and 8.0−8.5 for proline iminopeptidase were determined. Both peptidases were strongly inhibited by p-chloromercuribenzoic acid, heavy metal ions and urea. The molecular weights were determined by gel filtration to be 56 and 204 kDa, respectively. The iminopeptidase was decomposed during SDS electrophoresis to four subunits of 50 kDa. Minor impurities of myrosinase- associated protein (~70 kDa) were found in both preparations. Preliminary data of their amino acid sequences showed similarities to those of aminopeptidases N (family M1) and proline iminopeptidases (family S33). © 1946 – 2014: Verlag der Zeitschrift für Naturforschung
abstractGer	Aminopeptidase, preferring phenylalanine-p-nitroanilide as substrate, and proline iminopeptidase, highly-specific for proline-p-nitroanilide, were isolated from cabbage leaves (Brassica oleraceae var. capitata). As pH optima, 7.2−7.5 for aminopeptidase activity and 8.0−8.5 for proline iminopeptidase were determined. Both peptidases were strongly inhibited by p-chloromercuribenzoic acid, heavy metal ions and urea. The molecular weights were determined by gel filtration to be 56 and 204 kDa, respectively. The iminopeptidase was decomposed during SDS electrophoresis to four subunits of 50 kDa. Minor impurities of myrosinase- associated protein (~70 kDa) were found in both preparations. Preliminary data of their amino acid sequences showed similarities to those of aminopeptidases N (family M1) and proline iminopeptidases (family S33). © 1946 – 2014: Verlag der Zeitschrift für Naturforschung
abstract_unstemmed	Aminopeptidase, preferring phenylalanine-p-nitroanilide as substrate, and proline iminopeptidase, highly-specific for proline-p-nitroanilide, were isolated from cabbage leaves (Brassica oleraceae var. capitata). As pH optima, 7.2−7.5 for aminopeptidase activity and 8.0−8.5 for proline iminopeptidase were determined. Both peptidases were strongly inhibited by p-chloromercuribenzoic acid, heavy metal ions and urea. The molecular weights were determined by gel filtration to be 56 and 204 kDa, respectively. The iminopeptidase was decomposed during SDS electrophoresis to four subunits of 50 kDa. Minor impurities of myrosinase- associated protein (~70 kDa) were found in both preparations. Preliminary data of their amino acid sequences showed similarities to those of aminopeptidases N (family M1) and proline iminopeptidases (family S33). © 1946 – 2014: Verlag der Zeitschrift für Naturforschung
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title_short	Characterization of an Aminopeptidase and a Proline Iminopeptidase from Cabbage Leaves
url	https://doi.org/10.1515/znc-2008-1-220
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author2	Dolashki, Alexander Altenberend, Florian Stevanovic, Stefan Voelter, Wolfgang Tchorbanov, Bozhidar
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