Biological Chemistry

Issue: Dec 1999

Volume 380, Number 12

Mitochondria-Derived and Extra-Mitochondrial Human Type-1 Porin Are Identical as Revealed by Amino Acid Sequencing and Electrophysiological Characterisation

Ulrike Stadtmüller,
Jana Eben-Brunnen,
Angela Schmid,
Dörte Hesse,
Simone Klebert,
Hartmut D. Kratzin,
Jan Hesse,
Bodo Zimmermann,
Susanne Reymann,
Friedrich P. Thinnes,
Roland Benz,
Hilde Götz,
Norbert Hilschmann
Citation Information. Biological Chemistry. Volume 380, Issue 12, Pages 1461–1466, ISSN (Print) 1431-6730, DOI: 10.1515/BC.1999.189, December 1999
Published Online: 01/06/2005

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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