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

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Názov:	Purification and Characterization of Two Voltage-Dependent Anion Channel Isoforms from Plant Seeds
Autori:	Abrecht, H, Wattiez, R, Ruysschaert, Jean Marie, Homblé, Fabrice
Zdroj:	Plant Physiology. 124:1181-1190
Informácie o vydavateľovi:	Oxford University Press (OUP), 2000.
Rok vydania:	2000
Predmety:	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
Popis:	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.
Druh dokumentu:	Article
Popis súboru:	1 full-text file(s): application/pdf
Jazyk:	English
ISSN:	1532-2548 0032-0889
DOI:	10.1104/pp.124.3.1181
Prístupová URL adresa:	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
Prístupové číslo:	edsair.doi.dedup.....bb6b72e0ac1e83423b74f0e52f5d209c
Databáza:	OpenAIRE

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Abstrakt:	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