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Mitochondria-Derived and Extra-Mitochondrial Human Type-1 Porin Are Identical as Revealed by Amino Acid Sequencing and Electrophysiological Characterisation
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Ulrike Stadtmüller
Veröffentlicht/Copyright:
1. Juni 2005
Abstract
In mammalian cells porin channels are localised in both mitochondrial outer membranes and extra-mitochondrial membranes. We isolated mitochondria-derived porin of a human lymphoblastoid B cell line, determined its amino acid sequence and characterised its channel properties. Interestingly, the amino acid sequence of this porin preparation and, correspondingly, its electrophysiological characteristics in a reconstituted system were identical to those of ‘Porin 31HL’, the human type-1 porin purified from a crude membrane preparation of the same cell line using a different purification protocol. The results raise questions about targeting, insertion and orientation of human type-1 porin in different membranes.
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Published Online: 2005-06-01
Published in Print: 1999-12-20
Copyright (c) 1999 by Walter de Gruyter GmbH & Co. KG
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- To Our Authors, Readers and Subscribers
- Editor's Note
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- Molecular Genetics of Dopa-Responsive Dystonia
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- Xylose Utilisation: Cloning and Characterisation of the Xylose Reductase from Candida tenuis
- Xylose Utilisation: Cloning and Characterisation of the Xylitol Dehydrogenase from Galactocandida mastotermitis
- Thermodynamic Properties and DNA Binding of the ParD Protein from the Broad Host-Range Plasmid RK2/RP4 Killing System
- Dipeptidyl Peptidase III from Rat Liver Cytosol: Purification, Molecular Cloning and Immunohistochemical Localization
- Genomic Expansion Across the Albumin Gene Family on Human Chromosome 4q Is Directional
- Comparison of the Tamoxifen Regulated Chimeric Cre Recombinases MerCreMer and CreMer
- The Human Cathepsin F Gene a Fusion Product between an Ancestral Cathepsin and Cystatin Gene
- Characterization of a New Member of the TNF Family Expressed on Antigen Presenting Cells
- Vascular Endothelial Growth Factor (VEGF) and Its Receptors in Tumor-Bearing Dogs
- Molecular Cloning and Characterization of a cDNA Encoding a Transferrin Homolog from Bombyx mori
- Mitochondria-Derived and Extra-Mitochondrial Human Type-1 Porin Are Identical as Revealed by Amino Acid Sequencing and Electrophysiological Characterisation
- Acknowledgement
- Content Index
- Author Index
- Subject Index
Artikel in diesem Heft
- To Our Authors, Readers and Subscribers
- Editor's Note
- A Chimpanzee Millennium
- Molecular Genetics of Dopa-Responsive Dystonia
- In Vitro Transcription of a TATA-Less Promoter: Negative Regulation by the Not1 Protein
- Fast Control of DNA Replication in Response to Hypoxia and to Inhibited Protein Synthesis in CCRF-CEM and HeLa Cells
- The Inhibition of NF-B Activation Pathways and the Induction of Apoptosis by Dithiocarbamates in T Cells Are Blocked by the Glutathione Precursor N-Acetyl-L-Cysteine
- Xylose Utilisation: Cloning and Characterisation of the Xylose Reductase from Candida tenuis
- Xylose Utilisation: Cloning and Characterisation of the Xylitol Dehydrogenase from Galactocandida mastotermitis
- Thermodynamic Properties and DNA Binding of the ParD Protein from the Broad Host-Range Plasmid RK2/RP4 Killing System
- Dipeptidyl Peptidase III from Rat Liver Cytosol: Purification, Molecular Cloning and Immunohistochemical Localization
- Genomic Expansion Across the Albumin Gene Family on Human Chromosome 4q Is Directional
- Comparison of the Tamoxifen Regulated Chimeric Cre Recombinases MerCreMer and CreMer
- The Human Cathepsin F Gene a Fusion Product between an Ancestral Cathepsin and Cystatin Gene
- Characterization of a New Member of the TNF Family Expressed on Antigen Presenting Cells
- Vascular Endothelial Growth Factor (VEGF) and Its Receptors in Tumor-Bearing Dogs
- Molecular Cloning and Characterization of a cDNA Encoding a Transferrin Homolog from Bombyx mori
- Mitochondria-Derived and Extra-Mitochondrial Human Type-1 Porin Are Identical as Revealed by Amino Acid Sequencing and Electrophysiological Characterisation
- Acknowledgement
- Content Index
- Author Index
- Subject Index
