Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase.
نویسندگان
چکیده
منابع مشابه
Tightly Bound Magnesium in Mitochondrial Adenosine Triphosphatase from Beef Heart*
Tightly bound magnesium was found in soluble, purified ATPase (F,) from beef heart mitochondria in the amount of 1 mol/mol of F1. Iron, zinc, cobalt, manganese, calcium, sodium, copper, and potassium were not tightly bound at stoichiometric levels. Removal of magnesium by chelating agents caused loss of ATPase activity. Removal of tightly bound nucleotide by gel filtration in 50% glycerolor 60 ...
متن کاملTightly bound magnesium in mitochondrial adenosine triphosphatase from beef heart.
Tightly bound magnesium was found in soluble, purified ATPase (F1) from beef heart mitochondria in the amount of 1 mol/mol of F1. Iron, zinc, cobalt, manganese, calcium, sodium, copper, and potassium were not tightly bound at stoichiometric levels. Removal of magnesium by chelating agents caused loss of ATPase activity. Removal of tightly bound nucleotide by gel filtration in 50% glycerol- or 6...
متن کاملCatalysis of partial reactions of ATP synthesis by beef heart mitochondrial adenosine triphosphatase.
We have found that when the ATP hydrolysis activity of beef heart mitochondrial adenosine triphosphatase (F1) is eliminated by either cold treatment or chemical modification, the enzyme attains the ability to catalyze the Pi in equilibrium ATP exchange reaction. The ATP hydrolysis activity of isolated F1 was lost upon chemical modification by phenyglyoxal, butanedione, or 7-chloro-4-nitrobenzen...
متن کاملThe presence of two hydrolytic sites on beef heart mitochondrial adenosine triphosphatase.
The ribose-modified nucleotides 2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate (TNP-ATP) and TNP-ADP were used to probe the catalytic sites on soluble beef heart mitochondrial adenosine triphosphatase (F1). Both compounds were potent competitive inhibitors of ATP hydrolysis catalyzed by F1, Ki = 5.5 and 10 nM, respectively, and by submitochondrial particles, Ki (TNP-ATP) = 21 nM. Both...
متن کاملAurovertin, a fluorescent probe of conformational change in beef heart mitochondrial adenosine triphosphatase.
Formation of a complex between aurovertin and soluble mitochondrial adenosine triphosphatase (FJ was accompanied by a 55-fold enhancement of fluorescence, an increase in the polarization of fluorescence from 0.278 for the free form to 0.375 for the bound form and a decrease in absorption at 366 nm. The fluorescence intensity of the complex was partially quenched by addition of ATP or Mg++ and e...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1977
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)40446-7