Research Interests: Biochemistry, Chemistry, Kinetics, Calcium, Mitochondria, and 15 moreMedicine, Magnesium, Potassium, Phosphorylation, Time Factors, Oxidative phosphorylation, Multienzyme complexes, Metal ion, American Chemical Society, Alcaligenes, Edetic Acid, Biochemistry and cell biology, Adenosine Triphosphate, ATP hydrolysis, and Medical biochemistry and metabolomics
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Abstract The 13S coupling factor of oxidative phosphorylation from Alcaligenes faecalis forms an unusually stable complex with ADP which can be isolated by simple gel filtration. Most preparations of enzyme exhibit an apparent binding... more
Abstract The 13S coupling factor of oxidative phosphorylation from Alcaligenes faecalis forms an unusually stable complex with ADP which can be isolated by simple gel filtration. Most preparations of enzyme exhibit an apparent binding ratio of 1 mol of ADP per mol of enzyme with a dissociation constant of approximately 15 μ m . One mol of adenylyl imidodiphosphate (AMP-PNP) also binds, with a dissociation constant of about 3 μ m . A constant could not be obtained from ATP binding studies because this nucleotide is hydrolyzed by the enzyme. Competition studies suggest that both ADP and AMP-PNP bind to the same site. Bound nucleotides are in a very slow equilibrium with free nucleotides, with a turnover time of 1–2 h. The rate of radionucleotide dissociation from the isolated enzyme-nucleotide complex increases when unlabeled nucleotide is added, suggesting that binding of nucleotide to one site on the enzyme allosterically promotes dissociation of nucleotide from another site. A nucleotide-induced “flip-flop” type of oscillation of the properties of the nucleotide binding sites on the coupling factor is proposed. From a comparison of the kinetic parameters of the intrinsic adenosinetriphosphatase activity and the nucleotide binding parameters of the enzyme population in toto, it is suggested that the enzyme exhibits functional polymorphism.
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Research Interests: Biochemistry, Chemistry, Polymorphism, Kinetics, Medicine, and 13 morePolyamines, Magnesium, ATPase, Temperature, Enzyme, Time Factors, Oxidative phosphorylation, Genetic Polymorphism, Molecular weight, Hydrogen-Ion Concentration, Alcaligenes, Biochemistry and cell biology, and Medical biochemistry and metabolomics
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Research Interests: Biochemistry, Kinetics, Calcium, Mitochondria, Magnesium, and 11 morePotassium, Time Factors, Oxidative phosphorylation, Multienzyme complexes, Metal ion, American Chemical Society, Alcaligenes, Edetic Acid, Biochemistry and cell biology, Adenosine Triphosphate, and Medical biochemistry and metabolomics
Research Interests:
Abstract The 13S coupling factor of oxidative phosphorylation from Alcaligenes faecalis forms an unusually stable complex with ADP which can be isolated by simple gel filtration. Most preparations of enzyme exhibit an apparent binding... more
Abstract The 13S coupling factor of oxidative phosphorylation from Alcaligenes faecalis forms an unusually stable complex with ADP which can be isolated by simple gel filtration. Most preparations of enzyme exhibit an apparent binding ratio of 1 mol of ADP per mol of enzyme with a dissociation constant of approximately 15 μ m . One mol of adenylyl imidodiphosphate (AMP-PNP) also binds, with a dissociation constant of about 3 μ m . A constant could not be obtained from ATP binding studies because this nucleotide is hydrolyzed by the enzyme. Competition studies suggest that both ADP and AMP-PNP bind to the same site. Bound nucleotides are in a very slow equilibrium with free nucleotides, with a turnover time of 1–2 h. The rate of radionucleotide dissociation from the isolated enzyme-nucleotide complex increases when unlabeled nucleotide is added, suggesting that binding of nucleotide to one site on the enzyme allosterically promotes dissociation of nucleotide from another site. A nucleotide-induced “flip-flop” type of oscillation of the properties of the nucleotide binding sites on the coupling factor is proposed. From a comparison of the kinetic parameters of the intrinsic adenosinetriphosphatase activity and the nucleotide binding parameters of the enzyme population in toto, it is suggested that the enzyme exhibits functional polymorphism.
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ABSTRACT
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PROBLEM TO BE SOLVED: To certainly adjust timing in which a test package reaches a flow cell. SOLUTION: This control method or device for controlling flows of a liquid section L, a first air section A, and a last air section A has plural... more
PROBLEM TO BE SOLVED: To certainly adjust timing in which a test package reaches a flow cell. SOLUTION: This control method or device for controlling flows of a liquid section L, a first air section A, and a last air section A has plural cycles each of which begins from suction of the first air section A and ends with suction of the last air section A. In each the cycle, the liquid section L and the air sections A are selectively sucked into a first fluid pipe 30. First, the liquid section L and the air sections A are transferred from the first fluid pipe 30 to a second fluid pipe 35. After the last air section A is transferred to the second fluid pipe 35, the volume of the last air section A in each the cycle is adjusted. Then, the liquid section L and the air sections A in each the cycle are transferred from the second fluid pipe 35 to a third fluid pipe. After the first air section A is transferred to the third fluid pipe, the volume of the first air section A in each the cycle i...