Coupling factor activity of the purified pea mitochondrial F"1-ATPase

Horak, A. ; Packer, M.

Amsterdam : Elsevier
ISSN:
0005-2728
Keywords:
(Pea) ; Chloroplast CF"1-ATPase ; Coupling factor ; Mitochondrial F"1-ATPase
Source:
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
Topics:
Biology
Chemistry and Pharmacology
Medicine
Physics
Type of Medium:
Electronic Resource
URL:
_version_ 1798292367590031361
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.
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