Porin of Rhodobacter capsulatus: Biochemical and Functional Characterization

Abstract The major outer membrane protein of Rhodobacter capsulatus 37 b4 (capsule-free) was isolated. Strong porin-activity was observed after reconstitution into artificial lipid bilayer membranes with a single channel conductance of 3.15 nS in Im KC1. The porin migrated as a broad, single band...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Woitzik, Daniela [verfasserIn] Weckesser, Jürgen Benz, Roland Stevanovic, Stefan Jung, Günther Rosenbusch, Jürg P.

Format:	Artikel

Erschienen:	1990

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

Übergeordnetes Werk:	Enthalten in: Zeitschrift für Naturforschung. C, Biosciences - Verlag der Zeitschrift für Naturforschung, 1973, 45(1990), 6 vom: 01. Juni, Seite 576-582
Übergeordnetes Werk:	volume:45 ; year:1990 ; number:6 ; day:01 ; month:06 ; pages:576-582

Links:	Volltext

DOI / URN:	10.1515/znc-1990-0602

Katalog-ID:	OLC2137060841

Internformat


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520			\|a Abstract The major outer membrane protein of Rhodobacter capsulatus 37 b4 (capsule-free) was isolated. Strong porin-activity was observed after reconstitution into artificial lipid bilayer membranes with a single channel conductance of 3.15 nS in Im KC1. The porin migrated as a broad, single band ($ M_{r} $ above 90,000) on sodium dodecyl sulfate polyacrylamide gel electro phoresis and dissociated into a single species of polypeptides ($ M_{r} $ 36,000) on treatment with EDTA (10 mM at 30 °C, 20 min) or by heating (100 °C, 5 min). Analytical ultracentrifugation studies demonstrated the native porin to be a trimer. The monomers chromatofocused as a single, sharp peak on fast performance liquid chromatography and only one band, corre sponding to an isoelectric point of about 4.0, was obtained on isoelectric focusing. Gas-phase sequencing of the 23 N-terminal residues revealed Glu-Val-Lys-Leu-Ser-Gly-Asp-Ala-Arg-Met-Gly-Val-Met-Tyr-Asn-Gly-Asp-Asp-X-Asn-Phe-Ser-Ser.
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Indexfelder

author_variant	d w dw j w jw r b rb s s ss g j gj j p r jp jpr
matchkey_str	article:09395075:1990----::oiorooatrasltsiceiaaducin
hierarchy_sort_str	1990
publishDate	1990
allfields	10.1515/znc-1990-0602 doi (DE-627)OLC2137060841 (DE-B1597)znc-1990-0602-p DE-627 ger DE-627 rakwb 500 VZ 570 VZ 12 ssgn BIODIV DE-30 fid Woitzik, Daniela verfasserin aut Porin of Rhodobacter capsulatus: Biochemical and Functional Characterization 1990 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © 1946 – 2014: Verlag der Zeitschrift für Naturforschung Abstract The major outer membrane protein of Rhodobacter capsulatus 37 b4 (capsule-free) was isolated. Strong porin-activity was observed after reconstitution into artificial lipid bilayer membranes with a single channel conductance of 3.15 nS in Im KC1. The porin migrated as a broad, single band ($ M_{r} $ above 90,000) on sodium dodecyl sulfate polyacrylamide gel electro phoresis and dissociated into a single species of polypeptides ($ M_{r} $ 36,000) on treatment with EDTA (10 mM at 30 °C, 20 min) or by heating (100 °C, 5 min). Analytical ultracentrifugation studies demonstrated the native porin to be a trimer. The monomers chromatofocused as a single, sharp peak on fast performance liquid chromatography and only one band, corre sponding to an isoelectric point of about 4.0, was obtained on isoelectric focusing. Gas-phase sequencing of the 23 N-terminal residues revealed Glu-Val-Lys-Leu-Ser-Gly-Asp-Ala-Arg-Met-Gly-Val-Met-Tyr-Asn-Gly-Asp-Asp-X-Asn-Phe-Ser-Ser. Weckesser, Jürgen aut Benz, Roland aut Stevanovic, Stefan aut Jung, Günther aut Rosenbusch, Jürg P. aut Enthalten in Zeitschrift für Naturforschung. C, Biosciences Verlag der Zeitschrift für Naturforschung, 1973 45(1990), 6 vom: 01. Juni, Seite 576-582 (DE-627)129307394 (DE-600)124636-7 (DE-576)014504936 0939-5075 nnns volume:45 year:1990 number:6 day:01 month:06 pages:576-582 https://doi.org/10.1515/znc-1990-0602 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_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_55 GBV_ILN_69 GBV_ILN_70 GBV_ILN_74 GBV_ILN_105 GBV_ILN_120 GBV_ILN_121 GBV_ILN_130 GBV_ILN_252 GBV_ILN_259 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2026 GBV_ILN_2221 GBV_ILN_2237 GBV_ILN_4012 GBV_ILN_4027 GBV_ILN_4028 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 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_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4315 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4321 GBV_ILN_4323 GBV_ILN_4700 AR 45 1990 6 01 06 576-582
spelling	10.1515/znc-1990-0602 doi (DE-627)OLC2137060841 (DE-B1597)znc-1990-0602-p DE-627 ger DE-627 rakwb 500 VZ 570 VZ 12 ssgn BIODIV DE-30 fid Woitzik, Daniela verfasserin aut Porin of Rhodobacter capsulatus: Biochemical and Functional Characterization 1990 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © 1946 – 2014: Verlag der Zeitschrift für Naturforschung Abstract The major outer membrane protein of Rhodobacter capsulatus 37 b4 (capsule-free) was isolated. Strong porin-activity was observed after reconstitution into artificial lipid bilayer membranes with a single channel conductance of 3.15 nS in Im KC1. The porin migrated as a broad, single band ($ M_{r} $ above 90,000) on sodium dodecyl sulfate polyacrylamide gel electro phoresis and dissociated into a single species of polypeptides ($ M_{r} $ 36,000) on treatment with EDTA (10 mM at 30 °C, 20 min) or by heating (100 °C, 5 min). Analytical ultracentrifugation studies demonstrated the native porin to be a trimer. The monomers chromatofocused as a single, sharp peak on fast performance liquid chromatography and only one band, corre sponding to an isoelectric point of about 4.0, was obtained on isoelectric focusing. Gas-phase sequencing of the 23 N-terminal residues revealed Glu-Val-Lys-Leu-Ser-Gly-Asp-Ala-Arg-Met-Gly-Val-Met-Tyr-Asn-Gly-Asp-Asp-X-Asn-Phe-Ser-Ser. Weckesser, Jürgen aut Benz, Roland aut Stevanovic, Stefan aut Jung, Günther aut Rosenbusch, Jürg P. aut Enthalten in Zeitschrift für Naturforschung. C, Biosciences Verlag der Zeitschrift für Naturforschung, 1973 45(1990), 6 vom: 01. Juni, Seite 576-582 (DE-627)129307394 (DE-600)124636-7 (DE-576)014504936 0939-5075 nnns volume:45 year:1990 number:6 day:01 month:06 pages:576-582 https://doi.org/10.1515/znc-1990-0602 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_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_55 GBV_ILN_69 GBV_ILN_70 GBV_ILN_74 GBV_ILN_105 GBV_ILN_120 GBV_ILN_121 GBV_ILN_130 GBV_ILN_252 GBV_ILN_259 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2026 GBV_ILN_2221 GBV_ILN_2237 GBV_ILN_4012 GBV_ILN_4027 GBV_ILN_4028 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 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_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4315 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4321 GBV_ILN_4323 GBV_ILN_4700 AR 45 1990 6 01 06 576-582
allfields_unstemmed	10.1515/znc-1990-0602 doi (DE-627)OLC2137060841 (DE-B1597)znc-1990-0602-p DE-627 ger DE-627 rakwb 500 VZ 570 VZ 12 ssgn BIODIV DE-30 fid Woitzik, Daniela verfasserin aut Porin of Rhodobacter capsulatus: Biochemical and Functional Characterization 1990 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © 1946 – 2014: Verlag der Zeitschrift für Naturforschung Abstract The major outer membrane protein of Rhodobacter capsulatus 37 b4 (capsule-free) was isolated. Strong porin-activity was observed after reconstitution into artificial lipid bilayer membranes with a single channel conductance of 3.15 nS in Im KC1. The porin migrated as a broad, single band ($ M_{r} $ above 90,000) on sodium dodecyl sulfate polyacrylamide gel electro phoresis and dissociated into a single species of polypeptides ($ M_{r} $ 36,000) on treatment with EDTA (10 mM at 30 °C, 20 min) or by heating (100 °C, 5 min). Analytical ultracentrifugation studies demonstrated the native porin to be a trimer. The monomers chromatofocused as a single, sharp peak on fast performance liquid chromatography and only one band, corre sponding to an isoelectric point of about 4.0, was obtained on isoelectric focusing. Gas-phase sequencing of the 23 N-terminal residues revealed Glu-Val-Lys-Leu-Ser-Gly-Asp-Ala-Arg-Met-Gly-Val-Met-Tyr-Asn-Gly-Asp-Asp-X-Asn-Phe-Ser-Ser. Weckesser, Jürgen aut Benz, Roland aut Stevanovic, Stefan aut Jung, Günther aut Rosenbusch, Jürg P. aut Enthalten in Zeitschrift für Naturforschung. C, Biosciences Verlag der Zeitschrift für Naturforschung, 1973 45(1990), 6 vom: 01. Juni, Seite 576-582 (DE-627)129307394 (DE-600)124636-7 (DE-576)014504936 0939-5075 nnns volume:45 year:1990 number:6 day:01 month:06 pages:576-582 https://doi.org/10.1515/znc-1990-0602 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_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_55 GBV_ILN_69 GBV_ILN_70 GBV_ILN_74 GBV_ILN_105 GBV_ILN_120 GBV_ILN_121 GBV_ILN_130 GBV_ILN_252 GBV_ILN_259 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2026 GBV_ILN_2221 GBV_ILN_2237 GBV_ILN_4012 GBV_ILN_4027 GBV_ILN_4028 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 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_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4315 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4321 GBV_ILN_4323 GBV_ILN_4700 AR 45 1990 6 01 06 576-582
allfieldsGer	10.1515/znc-1990-0602 doi (DE-627)OLC2137060841 (DE-B1597)znc-1990-0602-p DE-627 ger DE-627 rakwb 500 VZ 570 VZ 12 ssgn BIODIV DE-30 fid Woitzik, Daniela verfasserin aut Porin of Rhodobacter capsulatus: Biochemical and Functional Characterization 1990 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © 1946 – 2014: Verlag der Zeitschrift für Naturforschung Abstract The major outer membrane protein of Rhodobacter capsulatus 37 b4 (capsule-free) was isolated. Strong porin-activity was observed after reconstitution into artificial lipid bilayer membranes with a single channel conductance of 3.15 nS in Im KC1. The porin migrated as a broad, single band ($ M_{r} $ above 90,000) on sodium dodecyl sulfate polyacrylamide gel electro phoresis and dissociated into a single species of polypeptides ($ M_{r} $ 36,000) on treatment with EDTA (10 mM at 30 °C, 20 min) or by heating (100 °C, 5 min). Analytical ultracentrifugation studies demonstrated the native porin to be a trimer. The monomers chromatofocused as a single, sharp peak on fast performance liquid chromatography and only one band, corre sponding to an isoelectric point of about 4.0, was obtained on isoelectric focusing. Gas-phase sequencing of the 23 N-terminal residues revealed Glu-Val-Lys-Leu-Ser-Gly-Asp-Ala-Arg-Met-Gly-Val-Met-Tyr-Asn-Gly-Asp-Asp-X-Asn-Phe-Ser-Ser. Weckesser, Jürgen aut Benz, Roland aut Stevanovic, Stefan aut Jung, Günther aut Rosenbusch, Jürg P. aut Enthalten in Zeitschrift für Naturforschung. C, Biosciences Verlag der Zeitschrift für Naturforschung, 1973 45(1990), 6 vom: 01. Juni, Seite 576-582 (DE-627)129307394 (DE-600)124636-7 (DE-576)014504936 0939-5075 nnns volume:45 year:1990 number:6 day:01 month:06 pages:576-582 https://doi.org/10.1515/znc-1990-0602 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_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_55 GBV_ILN_69 GBV_ILN_70 GBV_ILN_74 GBV_ILN_105 GBV_ILN_120 GBV_ILN_121 GBV_ILN_130 GBV_ILN_252 GBV_ILN_259 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2026 GBV_ILN_2221 GBV_ILN_2237 GBV_ILN_4012 GBV_ILN_4027 GBV_ILN_4028 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 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_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4315 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4321 GBV_ILN_4323 GBV_ILN_4700 AR 45 1990 6 01 06 576-582
allfieldsSound	10.1515/znc-1990-0602 doi (DE-627)OLC2137060841 (DE-B1597)znc-1990-0602-p DE-627 ger DE-627 rakwb 500 VZ 570 VZ 12 ssgn BIODIV DE-30 fid Woitzik, Daniela verfasserin aut Porin of Rhodobacter capsulatus: Biochemical and Functional Characterization 1990 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © 1946 – 2014: Verlag der Zeitschrift für Naturforschung Abstract The major outer membrane protein of Rhodobacter capsulatus 37 b4 (capsule-free) was isolated. Strong porin-activity was observed after reconstitution into artificial lipid bilayer membranes with a single channel conductance of 3.15 nS in Im KC1. The porin migrated as a broad, single band ($ M_{r} $ above 90,000) on sodium dodecyl sulfate polyacrylamide gel electro phoresis and dissociated into a single species of polypeptides ($ M_{r} $ 36,000) on treatment with EDTA (10 mM at 30 °C, 20 min) or by heating (100 °C, 5 min). Analytical ultracentrifugation studies demonstrated the native porin to be a trimer. The monomers chromatofocused as a single, sharp peak on fast performance liquid chromatography and only one band, corre sponding to an isoelectric point of about 4.0, was obtained on isoelectric focusing. Gas-phase sequencing of the 23 N-terminal residues revealed Glu-Val-Lys-Leu-Ser-Gly-Asp-Ala-Arg-Met-Gly-Val-Met-Tyr-Asn-Gly-Asp-Asp-X-Asn-Phe-Ser-Ser. Weckesser, Jürgen aut Benz, Roland aut Stevanovic, Stefan aut Jung, Günther aut Rosenbusch, Jürg P. aut Enthalten in Zeitschrift für Naturforschung. C, Biosciences Verlag der Zeitschrift für Naturforschung, 1973 45(1990), 6 vom: 01. Juni, Seite 576-582 (DE-627)129307394 (DE-600)124636-7 (DE-576)014504936 0939-5075 nnns volume:45 year:1990 number:6 day:01 month:06 pages:576-582 https://doi.org/10.1515/znc-1990-0602 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_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_55 GBV_ILN_69 GBV_ILN_70 GBV_ILN_74 GBV_ILN_105 GBV_ILN_120 GBV_ILN_121 GBV_ILN_130 GBV_ILN_252 GBV_ILN_259 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2026 GBV_ILN_2221 GBV_ILN_2237 GBV_ILN_4012 GBV_ILN_4027 GBV_ILN_4028 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 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_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4315 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4321 GBV_ILN_4323 GBV_ILN_4700 AR 45 1990 6 01 06 576-582
source	Enthalten in Zeitschrift für Naturforschung. C, Biosciences 45(1990), 6 vom: 01. Juni, Seite 576-582 volume:45 year:1990 number:6 day:01 month:06 pages:576-582
sourceStr	Enthalten in Zeitschrift für Naturforschung. C, Biosciences 45(1990), 6 vom: 01. Juni, Seite 576-582 volume:45 year:1990 number:6 day:01 month:06 pages:576-582
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title	Porin of Rhodobacter capsulatus: Biochemical and Functional Characterization
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title_full	Porin of Rhodobacter capsulatus: Biochemical and Functional Characterization
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title_sort	porin of rhodobacter capsulatus: biochemical and functional characterization
title_auth	Porin of Rhodobacter capsulatus: Biochemical and Functional Characterization
abstract	Abstract The major outer membrane protein of Rhodobacter capsulatus 37 b4 (capsule-free) was isolated. Strong porin-activity was observed after reconstitution into artificial lipid bilayer membranes with a single channel conductance of 3.15 nS in Im KC1. The porin migrated as a broad, single band ($ M_{r} $ above 90,000) on sodium dodecyl sulfate polyacrylamide gel electro phoresis and dissociated into a single species of polypeptides ($ M_{r} $ 36,000) on treatment with EDTA (10 mM at 30 °C, 20 min) or by heating (100 °C, 5 min). Analytical ultracentrifugation studies demonstrated the native porin to be a trimer. The monomers chromatofocused as a single, sharp peak on fast performance liquid chromatography and only one band, corre sponding to an isoelectric point of about 4.0, was obtained on isoelectric focusing. Gas-phase sequencing of the 23 N-terminal residues revealed Glu-Val-Lys-Leu-Ser-Gly-Asp-Ala-Arg-Met-Gly-Val-Met-Tyr-Asn-Gly-Asp-Asp-X-Asn-Phe-Ser-Ser. © 1946 – 2014: Verlag der Zeitschrift für Naturforschung
abstractGer	Abstract The major outer membrane protein of Rhodobacter capsulatus 37 b4 (capsule-free) was isolated. Strong porin-activity was observed after reconstitution into artificial lipid bilayer membranes with a single channel conductance of 3.15 nS in Im KC1. The porin migrated as a broad, single band ($ M_{r} $ above 90,000) on sodium dodecyl sulfate polyacrylamide gel electro phoresis and dissociated into a single species of polypeptides ($ M_{r} $ 36,000) on treatment with EDTA (10 mM at 30 °C, 20 min) or by heating (100 °C, 5 min). Analytical ultracentrifugation studies demonstrated the native porin to be a trimer. The monomers chromatofocused as a single, sharp peak on fast performance liquid chromatography and only one band, corre sponding to an isoelectric point of about 4.0, was obtained on isoelectric focusing. Gas-phase sequencing of the 23 N-terminal residues revealed Glu-Val-Lys-Leu-Ser-Gly-Asp-Ala-Arg-Met-Gly-Val-Met-Tyr-Asn-Gly-Asp-Asp-X-Asn-Phe-Ser-Ser. © 1946 – 2014: Verlag der Zeitschrift für Naturforschung
abstract_unstemmed	Abstract The major outer membrane protein of Rhodobacter capsulatus 37 b4 (capsule-free) was isolated. Strong porin-activity was observed after reconstitution into artificial lipid bilayer membranes with a single channel conductance of 3.15 nS in Im KC1. The porin migrated as a broad, single band ($ M_{r} $ above 90,000) on sodium dodecyl sulfate polyacrylamide gel electro phoresis and dissociated into a single species of polypeptides ($ M_{r} $ 36,000) on treatment with EDTA (10 mM at 30 °C, 20 min) or by heating (100 °C, 5 min). Analytical ultracentrifugation studies demonstrated the native porin to be a trimer. The monomers chromatofocused as a single, sharp peak on fast performance liquid chromatography and only one band, corre sponding to an isoelectric point of about 4.0, was obtained on isoelectric focusing. Gas-phase sequencing of the 23 N-terminal residues revealed Glu-Val-Lys-Leu-Ser-Gly-Asp-Ala-Arg-Met-Gly-Val-Met-Tyr-Asn-Gly-Asp-Asp-X-Asn-Phe-Ser-Ser. © 1946 – 2014: Verlag der Zeitschrift für Naturforschung
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title_short	Porin of Rhodobacter capsulatus: Biochemical and Functional Characterization
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