Coupling factor activity of the purified pea mitochondrial F"1-ATPase
ISSN: |
0005-2728
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Keywords: |
(Pea) ; Chloroplast CF"1-ATPase ; Coupling factor ; Mitochondrial F"1-ATPase
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Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
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Topics: |
Biology
Chemistry and Pharmacology
Medicine
Physics
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Type of Medium: |
Electronic Resource
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URL: |
_version_ | 1798292367590031361 |
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autor | Horak, A. Packer, M. |
autorsonst | Horak, A. Packer, M. |
book_url | http://linkinghub.elsevier.com/retrieve/pii/0005-2728(85)90215-4 |
datenlieferant | nat_lic_papers |
fussnote | The pea cotyledon mitochondrial F"1-ATPase was released from the submitochondrial particles by a washing procedure using 300 mM sucrose /2 mM Tricine (pH 7.4). The enzyme was purified by DEAE-cellulose chromatography and subsequent sucrose density gradient centrifugation. Using polyacrylamide gel electrophoresis under non-denaturing conditions, the purified protein exhibited a single sharp band with slightly lower mobility than the purified pea chloroplast CF"1-ATPase. The molecular weights of pea mitochondrial F"1-ATPase and pea chloroplast CF"1-ATPase were found to be 409 000 and 378 000, respectively. The purified pea mitochondrial F"1-ATPase dissociated into six types of subunits on polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Most of these subunits had mobilities different from the subunits of the pea chloroplast CF"1-ATPase. The purified mitochondrial F"1-ATPase exhibited coupling factor activity. In spite of the observed differences between CF"1 and F"1, the mitochondrial enzyme stimulated ATP formation in CF"1-depleted pea chloroplast membranes. Thus, the mitochondrial F"1 was able to substitute functionally for the chloroplast CF"1 in reconstituting photophosphorylation. |
hauptsatz | hsatz_simple |
identnr | NLZ185693822 |
issn | 0005-2728 |
journal_name | Biochimica et Biophysica Acta (BBA)/Bioenergetics |
materialart | 1 |
package_name | Elsevier |
publikationsort | Amsterdam |
publisher | Elsevier |
reference | 810 (1985), S. 310-318 |
schlagwort | (Pea) Chloroplast CF"1-ATPase Coupling factor Mitochondrial F"1-ATPase |
search_space | articles |
shingle_author_1 | Horak, A. Packer, M. |
shingle_author_2 | Horak, A. Packer, M. |
shingle_author_3 | Horak, A. Packer, M. |
shingle_author_4 | Horak, A. Packer, M. |
shingle_catch_all_1 | Horak, A. Packer, M. Coupling factor activity of the purified pea mitochondrial F"1-ATPase (Pea) Chloroplast CF"1-ATPase Coupling factor Mitochondrial F"1-ATPase (Pea) Chloroplast CF"1-ATPase Coupling factor Mitochondrial F"1-ATPase 0005-2728 00052728 Elsevier |
shingle_catch_all_2 | Horak, A. Packer, M. Coupling factor activity of the purified pea mitochondrial F"1-ATPase (Pea) Chloroplast CF"1-ATPase Coupling factor Mitochondrial F"1-ATPase (Pea) Chloroplast CF"1-ATPase Coupling factor Mitochondrial F"1-ATPase 0005-2728 00052728 Elsevier |
shingle_catch_all_3 | Horak, A. Packer, M. Coupling factor activity of the purified pea mitochondrial F"1-ATPase (Pea) Chloroplast CF"1-ATPase Coupling factor Mitochondrial F"1-ATPase (Pea) Chloroplast CF"1-ATPase Coupling factor Mitochondrial F"1-ATPase 0005-2728 00052728 Elsevier |
shingle_catch_all_4 | Horak, A. Packer, M. Coupling factor activity of the purified pea mitochondrial F"1-ATPase (Pea) Chloroplast CF"1-ATPase Coupling factor Mitochondrial F"1-ATPase (Pea) Chloroplast CF"1-ATPase Coupling factor Mitochondrial F"1-ATPase 0005-2728 00052728 Elsevier |
shingle_title_1 | Coupling factor activity of the purified pea mitochondrial F"1-ATPase |
shingle_title_2 | Coupling factor activity of the purified pea mitochondrial F"1-ATPase |
shingle_title_3 | Coupling factor activity of the purified pea mitochondrial F"1-ATPase |
shingle_title_4 | Coupling factor activity of the purified pea mitochondrial F"1-ATPase |
sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
timestamp | 2024-05-06T08:47:23.449Z |
titel | Coupling factor activity of the purified pea mitochondrial F"1-ATPase |
titel_suche | Coupling factor activity of the purified pea mitochondrial F"1-ATPase The pea cotyledon mitochondrial F"1-ATPase was released from the submitochondrial particles by a washing procedure using 300 mM sucrose /2 mM Tricine (pH 7.4). The enzyme was purified by DEAE-cellulose chromatography and subsequent sucrose density gradient centrifugation. Using polyacrylamide gel electrophoresis under non-denaturing conditions, the purified protein exhibited a single sharp band with slightly lower mobility than the purified pea chloroplast CF"1-ATPase. The molecular weights of pea mitochondrial F"1-ATPase and pea chloroplast CF"1-ATPase were found to be 409 000 and 378 000, respectively. The purified pea mitochondrial F"1-ATPase dissociated into six types of subunits on polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Most of these subunits had mobilities different from the subunits of the pea chloroplast CF"1-ATPase. The purified mitochondrial F"1-ATPase exhibited coupling factor activity. In spite of the observed differences between CF"1 and F"1, the mitochondrial enzyme stimulated ATP formation in CF"1-depleted pea chloroplast membranes. Thus, the mitochondrial F"1 was able to substitute functionally for the chloroplast CF"1 in reconstituting photophosphorylation. |
topic | W V WW-YZ U |
uid | nat_lic_papers_NLZ185693822 |