3P147 Site occupancy and ATP hydrolysis activity of F_1-ATPase without noncatalytic nucleotide binding site
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چکیده
منابع مشابه
آنالیز پروفایل nbs (nucleotide binding-site) ژنهای مقاومت به بیماری در ارقام مختلف زیتون
به منظور مطالعه ژنهای مقاومت nbs-lrr و تنوع ژنتیکی آنها در بین ارقام بومی زیتون و همچنین مقایسه آن با ارقام خارجی، از تکنیک profiling nbs و آنالیزهای مولکولی استفاده شد. برای این منظور dna ژنومی تعداد 5 رقم خارجی و 5 رقم داخلی زیتون استخراج و با آنزیم های برشی alui و rsai هضم و با استفاده از 3 آغازگر دژنره( nbs2،nbs7،nbs5a) در دو مرحله تکثیر شدند و الگوی باندی حاصل از تکثیر انتخابی آنها در روی ...
Adenine nucleotide binding sites on beef heart F1 ATPase: photoaffinity labeling of beta-subunit Tyr-368 at a noncatalytic site and beta Tyr-345 at a catalytic site.
2-Azidoadenine [32P]nucleotide was bound specifically at catalytic or noncatalytic nucleotide binding sites on beef heart mitochondrial F1 ATPase. In both cases, photolysis resulted in nearly exclusive labeling of the beta subunit. The modified enzyme was digested with trypsin, and labeled peptides were purified by reversed-phase high-pressure liquid chromatography. Amino acid sequence analysis...
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Site-directed mutagenesis was applied to modify phenylalanines (Phe(475)Trp, Phe(548)Tyr, and both) to generate mutants on the basis of molecular modeling of the ATP-binding domain of Na(+)/K(+)-ATPase, in order to characterize the forces that stabilize ATP in its binding pocket. Each of the mutants was examined by Raman difference spectroscopy, i.e., as a difference between the spectrum of the...
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Michel Ronjat, Jean Jacques Lacapere$, Jean-Pierre Dufourp, and Yves Dupont From the Luboratoire de Bwphysique Mol=Gculaire et Cellulaire, Centre d’Etudes Nuckaires de Grenoble, 3804l-Grenoble, France, the $Service de Biophysique, Departement de Biologic, Centre d’Etudes Nuckaires de Saclay, 91190-Gif-sur-Yuette, France, and the ILabOratoire des Sciences et Technologies Brassicoles, Uniuersite ...
متن کاملIsolation of subunits from Methanosarcina barkeri ATPase: nucleotide-binding site in the alpha subunit.
The alpha (62,000-dalton) and beta (49,000-dalton) subunits of Methanosarcina barkeri ATPase were purified to homogeneity. The subunits and ATPase complex were trypsinized in the presence of various nucleotides. ATP and ADP changed the trypsin sensitivity of the alpha subunit in the complex and isolated forms, suggesting the presence of a nucleotide-binding site in the alpha subunit.
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2004
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.44.s226_3