S1.8 Affinity purification of F-ATPases from mitochondria
                    
                        
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                    چکیده
منابع مشابه
The affinity purification and characterization of ATP synthase complexes from mitochondria
The mitochondrial F₁-ATPase inhibitor protein, IF₁, inhibits the hydrolytic, but not the synthetic activity of the F-ATP synthase, and requires the hydrolysis of ATP to form the inhibited complex. In this complex, the α-helical inhibitory region of the bound IF₁ occupies a deep cleft in one of the three catalytic interfaces of the enzyme. Its N-terminal region penetrates into the central aqueou...
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1. alpha-Cyano-4-hydroxycinnamate was coupled to Sepharose CL-4B activated with 1,2:3,4-bisepoxybutane. 2. The low-Km rat liver mitochondrial aldehyde dehydrogenase was specifically bound to this affinity medium, and could subsequently be eluted with alpha-cyano-4-hydroxycinnamate. 3. The enzyme purified in this manner had a subunit molecular mass of 55 kDa and a pI of approx. 6.5. A minor comp...
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Mersalyl is a powerful inhibitor of phosphate transport in mitochondria. In addition, by its reversible reaction with thiol groups, it can protect the latter from irreversible reaction with N-ethylmaleimide [ 1,2]. Use of this property enabled a group of proteins of M, 3.0-3.2 X lo4 to be identified in the internal mitochondrial membrane [3-g]. This group of proteins could be directly labeled u...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Bioenergetics
سال: 2008
ISSN: 0005-2728
DOI: 10.1016/j.bbabio.2008.05.046