[12] The large-scale preparation and properties of heart mitochondria from slaughterhouse material

Blair, P.V.

doi:10.1016/0076-6879(67)10015-3

Cited by 109 publications

(27 citation statements)

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“…Mitochondria were isolated from beef heart either by a modification [6] of the procedure described by Hatefi et al [7] or a modification of the procedure described by Blair [8]. Submitochondrial particles were prepared by ultrasonic disruption of mitochondria [9].…”

Section: Methodsmentioning

confidence: 99%

On the sigmoidal relationship between inhibition of respiration and antimycin titer

Rieske

Gupta

1972

FEBS Letters

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Section: Methodsmentioning

confidence: 99%

On the sigmoidal relationship between inhibition of respiration and antimycin titer

Rieske

Gupta

1972

FEBS Letters

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“…Lyophilized mitochondria (3.85 g) were isolated from a fresh beef heart (2.4 kg) by established protocols [32]. The lyophilisate was heated in CHC1, for 7 d at reflux, filtered and the solvent evaporated, yielding 0.26 g brown oil.…”

Section: Isolation Of P(3-hb) From Beef-heart Mitochondriamentioning

confidence: 99%

Isolation and ¹H‐NMR Spectroscopic Identification of Poly(3‐Hydroxybutanoate) from Prokaryotic and Eukaryotic Organisms

Seebàch

Brunner

Bürger

et al. 1994

European Journal of Biochemistry

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Trace amounts of poly[(R)‐3‐hydroxybutanoate] were isolated from competent Escherichia coli, spinach, bovine serum albumin, beef heart mitochondria, and aortal tissues, all sources in which it is not accumulated as storage material. Its identity was in all cases proved by 1H‐NMR spectroscopy. In some runs, the poly[(R)‐3‐hydroxybutanoate] isolated from competent E. coli also contained some 3‐hydroxyvalerate, an observation confirmed by 1H‐NMR spectroscopy and gas chromatography. The absolute configuration of the polymers isolated from E. coli and spinach was shown to be (all‐R) by gas chromatography on chiral columns.

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“…Beef heart mitochondria were isolated essentially according to Blair [16] in 0.25 M sucrose, 10 mM Tris-HC1, 0.05 mM EDTA, pH 7.4, and washed twice.…”

Section: Preparationsmentioning

confidence: 99%

Isolation of the ADP/ATP Translocator from Beef Heart Mitochondria as the Bongkrekate‐Protein Complex

Aquila

Eiermann

Babel

et al. 1978

European Journal of Biochemistry

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1. The isolation of the ADPiATP translocator from beef heart mitochondria as the bongkrekateprotein complex is described, using hydroxyapatite chromatography and gel filtration in Triton X-100 solution.2. The inhibitor is bound to the protein prior to solubilization with detergent for protection against denaturation. Only the intact bongkrekate-protein passes easily through the hydroxyapatite column. Bongkrekate shields the protein in contrast to carboxyatractylate only partially against proteinases present in the crude extract.3. The isolated bongkrekate protein shows the same molecular weights in dodecylsulfate and Triton X-100, the same amino acid composition and the same isoelectric point as the earlier isolated carboxyatractylate-protein complex. It differs by its higher sensitivity against trypsin and thermolysin.4. The identity of both proteins is demonstrated by interconversion of the bongkrekate-protein into the carboxyatractylate-protein. The process requires the catalysis by ADP or ATP, the natural substrates of the protein.5. The formation of the extractable [3H]bongkrekate-protein complex in mitochondria requires the presence of ADP or ATP.6. These data, the immunological studies presented earlier, and the differences in the reactivity of -SH groups of the isolated bongkrekate and carboxyatractylate complexes (to be published) indicate that both proteins represent different conformational states of the translocator protein (m-state and c-state).The isolation of the most active transport carrier of biomembranes in aerobic eukaryotic cell, the mitochondrial ADP/ATP translocator, has been reported by us recently [I -31. The protein was isolated in undenatured form as the carboxyatractylate-protein complex and turned out, in agreement with its eminent role, to be also the most prominent polypeptide of mitochondria and the most abundant membrane protein in heart and probably many other aerobic eukaryotic cells.' A unique feature of this translocator is the existence of two types of tightly binding inhibitors, carboxyatractylate and its homologues and bongkrekate [4,5], the application of which permitted to give a first insight into the molecular mechanism of a translocation process. Thus opposite effects of both ligands on the ADP binding to the carrier were observed: whereas carboxyatractylate removed ADP, bongkrekate appeared to increase the affinity of ADP [6,7]. This effect and a number of other results could be explained by the reorientation mechanism which implies that the translocator exists in two extremes of conformations largely identical with the translocation step [I, 8,9] ; in the 'c-state' where the substrate binding site is turned to the cytosol, and in the 'mstate' where the site is turned to the matrix. Transition between both states occurs only in the presence of ADP or ATP accompanied by the transport of the substrates across the membrane. The c-state can be fixed by binding carboxyatractylate and the m-state by binding bongkrekate.The isolation of the bongkrekate complex of the carri...

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[12] The large-scale preparation and properties of heart mitochondria from slaughterhouse material

Cited by 109 publications

References 3 publications

On the sigmoidal relationship between inhibition of respiration and antimycin titer

On the sigmoidal relationship between inhibition of respiration and antimycin titer

Isolation and ¹H‐NMR Spectroscopic Identification of Poly(3‐Hydroxybutanoate) from Prokaryotic and Eukaryotic Organisms

Isolation of the ADP/ATP Translocator from Beef Heart Mitochondria as the Bongkrekate‐Protein Complex

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[12] The large-scale preparation and properties of heart mitochondria from slaughterhouse material

Cited by 109 publications

References 3 publications

On the sigmoidal relationship between inhibition of respiration and antimycin titer

On the sigmoidal relationship between inhibition of respiration and antimycin titer

Isolation and 1H‐NMR Spectroscopic Identification of Poly(3‐Hydroxybutanoate) from Prokaryotic and Eukaryotic Organisms

Isolation of the ADP/ATP Translocator from Beef Heart Mitochondria as the Bongkrekate‐Protein Complex

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Isolation and ¹H‐NMR Spectroscopic Identification of Poly(3‐Hydroxybutanoate) from Prokaryotic and Eukaryotic Organisms