In:
Zeitschrift für Naturforschung C, Walter de Gruyter GmbH, Vol. 45, No. 6 ( 1990-6-1), p. 576-582
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.
Type of Medium:
Online Resource
ISSN:
1865-7125
,
0939-5075
DOI:
10.1515/znc-1990-0602
Language:
English
Publisher:
Walter de Gruyter GmbH
Publication Date:
1990
detail.hit.zdb_id:
2078107-6
SSG:
12
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