Studies on the relationship between the inner and outer membranes of rat liver mitochondria as determined by subfractionation with digitonin
| ISSN: |
0003-9861
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|---|---|
| Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
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| Topics: |
Biology
Chemistry and Pharmacology
Physics
|
| Type of Medium: |
Electronic Resource
|
| URL: |
| _version_ | 1798292197600133120 |
|---|---|
| autor | Jancsik, V. Linden, M. Dorbani, L. Rendon, A. Nelson, B.D. |
| autorsonst | Jancsik, V. Linden, M. Dorbani, L. Rendon, A. Nelson, B.D. |
| book_url | http://dx.doi.org/10.1016/0003-9861(88)90597-8 |
| datenlieferant | nat_lic_papers |
| fussnote | The present investigation has attempted to define in rat liver mitochondria the distribution of outer membrane proteins in relation to the inner membrane by fractionation with digitonin and phospholipase A"2. Porin, the channel-forming protein in the outer membrane, was measured quantitatively by immunological methods. Neither monoamine oxidase nor porin could be released by phospholipase A"2 treatment, but both were released by digitonin, at the same detergent concentration. Thus, the release of monoamine oxidase and porin requires the disruption of the cholesterol but not the phospholipid domains of the membrane and the two polypeptides exist in the same, or similar, membrane environment with regard to cholesterol. Changes in the energy state, or binding of brain hexokinase to rat liver mitochondria prior to fractionation with digitonin, did not alter the release patterns of porin and monoamine oxidase. The uptake of Ca^2^+, however, resulted in the concomitant release of the outer membrane markers together with the matrix marker, malate dehydrogenase. The present findings with liver differ from those obtained recently with brain mitochondria (L. Dorbani et al. (1987) Arch. Biochem. Biophys. 252, 188-196) in which two populations of porin were located in two different cholesterol domains. The significance of these differences in the location of porin in liver and brain mitochondria is discussed. |
| hauptsatz | hsatz_simple |
| identnr | NLZ183442741 |
| issn | 0003-9861 |
| journal_name | Archives of Biochemistry and Biophysics |
| materialart | 1 |
| package_name | Elsevier |
| publikationsort | Amsterdam |
| publisher | Elsevier |
| reference | 264 (1988), S. 295-301 |
| search_space | articles |
| shingle_author_1 | Jancsik, V. Linden, M. Dorbani, L. Rendon, A. Nelson, B.D. |
| shingle_author_2 | Jancsik, V. Linden, M. Dorbani, L. Rendon, A. Nelson, B.D. |
| shingle_author_3 | Jancsik, V. Linden, M. Dorbani, L. Rendon, A. Nelson, B.D. |
| shingle_author_4 | Jancsik, V. Linden, M. Dorbani, L. Rendon, A. Nelson, B.D. |
| shingle_catch_all_1 | Jancsik, V. Linden, M. Dorbani, L. Rendon, A. Nelson, B.D. Studies on the relationship between the inner and outer membranes of rat liver mitochondria as determined by subfractionation with digitonin 0003-9861 00039861 Elsevier |
| shingle_catch_all_2 | Jancsik, V. Linden, M. Dorbani, L. Rendon, A. Nelson, B.D. Studies on the relationship between the inner and outer membranes of rat liver mitochondria as determined by subfractionation with digitonin 0003-9861 00039861 Elsevier |
| shingle_catch_all_3 | Jancsik, V. Linden, M. Dorbani, L. Rendon, A. Nelson, B.D. Studies on the relationship between the inner and outer membranes of rat liver mitochondria as determined by subfractionation with digitonin 0003-9861 00039861 Elsevier |
| shingle_catch_all_4 | Jancsik, V. Linden, M. Dorbani, L. Rendon, A. Nelson, B.D. Studies on the relationship between the inner and outer membranes of rat liver mitochondria as determined by subfractionation with digitonin 0003-9861 00039861 Elsevier |
| shingle_title_1 | Studies on the relationship between the inner and outer membranes of rat liver mitochondria as determined by subfractionation with digitonin |
| shingle_title_2 | Studies on the relationship between the inner and outer membranes of rat liver mitochondria as determined by subfractionation with digitonin |
| shingle_title_3 | Studies on the relationship between the inner and outer membranes of rat liver mitochondria as determined by subfractionation with digitonin |
| shingle_title_4 | Studies on the relationship between the inner and outer membranes of rat liver mitochondria as determined by subfractionation with digitonin |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| timestamp | 2024-05-06T08:44:41.584Z |
| titel | Studies on the relationship between the inner and outer membranes of rat liver mitochondria as determined by subfractionation with digitonin |
| titel_suche | Studies on the relationship between the inner and outer membranes of rat liver mitochondria as determined by subfractionation with digitonin The present investigation has attempted to define in rat liver mitochondria the distribution of outer membrane proteins in relation to the inner membrane by fractionation with digitonin and phospholipase A"2. Porin, the channel-forming protein in the outer membrane, was measured quantitatively by immunological methods. Neither monoamine oxidase nor porin could be released by phospholipase A"2 treatment, but both were released by digitonin, at the same detergent concentration. Thus, the release of monoamine oxidase and porin requires the disruption of the cholesterol but not the phospholipid domains of the membrane and the two polypeptides exist in the same, or similar, membrane environment with regard to cholesterol. Changes in the energy state, or binding of brain hexokinase to rat liver mitochondria prior to fractionation with digitonin, did not alter the release patterns of porin and monoamine oxidase. The uptake of Ca^2^+, however, resulted in the concomitant release of the outer membrane markers together with the matrix marker, malate dehydrogenase. The present findings with liver differ from those obtained recently with brain mitochondria (L. Dorbani et al. (1987) Arch. Biochem. Biophys. 252, 188-196) in which two populations of porin were located in two different cholesterol domains. The significance of these differences in the location of porin in liver and brain mitochondria is discussed. |
| topic | W V U |
| uid | nat_lic_papers_NLZ183442741 |