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Purification and Characterization of Two Voltage-Dependent Anion Channel Isoforms from Plant Seeds

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Bibliographic Details
Title: Purification and Characterization of Two Voltage-Dependent Anion Channel Isoforms from Plant Seeds
Authors: Abrecht, H, Wattiez, R, Ruysschaert, Jean Marie, Homblé, Fabrice
Source: Plant Physiology. 124:1181-1190
Publisher Information: Oxford University Press (OUP), 2000.
Publication Year: 2000
Subject Terms: Fabaceae -- ultrastructure, 0301 basic medicine, Seeds -- metabolism, Lipid Bilayers, Molecular Sequence Data, Porins, Ion Channels -- chemistry, Medicinal, Peptide Mapping, Ion Channels, 03 medical and health sciences, Mitochondria -- metabolism, Sequence Analysis, Protein, Fabaceae -- chemistry, Lipid Bilayers -- chemistry, Phosphatidylcholines -- chemistry, Plant Proteins -- isolation & purification, Protein Isoforms, Voltage-Dependent Anion Channels, Amino Acid Sequence, Plant Proteins, 0303 health sciences, Porins -- chemistry, Plants, Medicinal, Ion Channels -- isolation & purification, Protein, Fabaceae, Mitochondria -- chemistry, Sciences bio-médicales et agricoles, Plants, Seeds -- ultrastructure, Mitochondria, Protein Isoforms -- chemistry, Porins -- isolation & purification, Seeds, Phosphatidylcholines, Protein Isoforms -- isolation & purification, Fabaceae -- metabolism, Seeds -- chemistry, Sequence Analysis, Sequence Alignment, Plant Proteins -- chemistry
Description: Mitochondria were isolated from imbibed seeds of lentil (Lens culinaris) and Phaseolus vulgaris. We copurified two voltage-dependent anion channel from detergent solubilized mitochondria in a single purification step using hydroxyapatite. The two isoforms from P. vulgaris were separated by chromatofocusing chromatography in 4m urea without any loss of channel activity. Channel activity of each isoform was characterized upon reconstitution into diphytanoyl phosphatidylcholine planar lipid bilayers. Both isoforms form large conductance channels that are slightly anion selective and display cation selective substates.
Document Type: Article
File Description: 1 full-text file(s): application/pdf
Language: English
ISSN: 1532-2548
0032-0889
DOI: 10.1104/pp.124.3.1181
Access URL: http://www.plantphysiol.org/content/124/3/1181.full.pdf
https://pubmed.ncbi.nlm.nih.gov/11080295
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/58318/Details
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC59217/
https://core.ac.uk/display/8857882
https://academic.oup.com/plphys/article/124/3/1181/6097514
https://www.jstor.org/stable/4279521
http://www.plantphysiol.org/content/124/3/1181
Rights: OUP Standard Publication Reuse
Accession Number: edsair.doi.dedup.....bb6b72e0ac1e83423b74f0e52f5d209c
Database: OpenAIRE
Description
Abstract:Mitochondria were isolated from imbibed seeds of lentil (Lens culinaris) and Phaseolus vulgaris. We copurified two voltage-dependent anion channel from detergent solubilized mitochondria in a single purification step using hydroxyapatite. The two isoforms from P. vulgaris were separated by chromatofocusing chromatography in 4m urea without any loss of channel activity. Channel activity of each isoform was characterized upon reconstitution into diphytanoyl phosphatidylcholine planar lipid bilayers. Both isoforms form large conductance channels that are slightly anion selective and display cation selective substates.
ISSN:15322548
00320889
DOI:10.1104/pp.124.3.1181