A Simplified Method for Estimating Urinary Inorganic Phosphate during Aluminum Gel Therapy for Phosphatic Calculi

Taussky, Hertha H.; Shorr, Ephraim

doi:10.1016/s0022-5347(17)68090-x

Cited by 44 publications

(43 citation statements)

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“…The protein content (9) and glycolytic enzymes like hexokinase (10), phosphoglucoisomerase (11), aldolase (12) and gluconeogenic enzymes like glucose-6phospha- tase (13)(14) and fructose-1,6-biphosphatase (15) were assayed. The nucleic acids from the tissues were extracted by the method of Schneider with trichloroacetic acid.…”

Section: Biochemical Analysismentioning

confidence: 99%

Anticarcinogenic Activity of Allylmercaptocaptopril Against Aflatoxin-B1 Induced Liver Carcinoma in Rats

et al. 2011

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Section: Biochemical Analysismentioning

confidence: 99%

Anticarcinogenic Activity of Allylmercaptocaptopril Against Aflatoxin-B1 Induced Liver Carcinoma in Rats

et al. 2011

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“…For determination of K M values, the same buffer was used, and the MgATP concentration was varied, keeping the MgSO 4 :ATP concentration constant at 1:2.5. Released inorganic phosphate (P i ) was determined as described (52,53). One unit is defined as 1 mol of ATP hydrolyzed (corresponding to 1 mol of P i produced) per min.…”

Section: Preparation Of Enzymes Functional Analysis Of Mutant Strainmentioning

confidence: 99%

Identification of the β _TP site in the x-ray structure of F ₁ -ATPase as the high-affinity catalytic site

Mao

Weber²

2007

Proc. Natl. Acad. Sci. U.S.A.

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ATP synthase uses a unique rotary mechanism to couple ATP synthesis and hydrolysis to transmembrane proton translocation. The F1 subcomplex has three catalytic nucleotide binding sites, one on each ␤ subunit, with widely differing affinities for MgATP or MgADP. During rotational catalysis, the sites switch their affinities. The affinity of each site is determined by the position of the central ␥ subunit. The site with the highest nucleotide binding affinity is catalytically active. From the available x-ray structures, it is not possible to discern the high-affinity site. Using fluorescence resonance energy transfer between tryptophan residues engineered into ␥ and trinitrophenyl nucleotide analogs on the catalytic sites, we were able to determine that the high-affinity site is close to the C-terminal helix of ␥, but at considerable distance from its N terminus. Thus, the ␤TP site in the ATP synthase ͉ catalytic mechanism ͉ rotation F 1 F o -ATP synthase is responsible for the bulk of ATP synthesis from ADP and P i in most organisms. F 1 F o -ATP synthase consists of the membrane embedded F o subcomplex with, in Escherichia coli, a subunit composition of ab 2 c 10 , and the peripheral F 1 subcomplex, with a subunit composition of ␣ 3 ␤ 3 ␥␦ . The energy necessary for ATP synthesis is derived from an electrochemical transmembrane proton (or, in some organisms, sodium ion) gradient. Proton flow, down the gradient, through F o is coupled to ATP synthesis on F 1 by a unique rotary mechanism. The protons flow through channels at the interface of a and c subunits, which drives rotation of the ring of c subunits. The c 10 ring, together with F 1 subunits ␥ and , forms the rotor. Rotation of ␥ leads to conformational changes in the catalytic nucleotide binding sites on the ␤ subunits, where ADP and P i are bound. The conformational changes result in formation and release of ATP. Thus, ATP synthase converts electrochemical energy, the proton gradient, into mechanical energy in form of subunit rotation, and back into chemical energy as ATP. In bacteria, under certain physiological conditions, the process runs in reverse. ATP is hydrolyzed to generate a transmembrane proton gradient which the bacterium requires for such functions as nutrient import and locomotion (for reviews, see refs.

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“…For the range from 5 to 0.5 mM the method of Rose and Liebowitz [8] was used. The inorganic phosphate, formed stoichiometrically from 2,3-P,glycerate was determined according to the method of Taussky and Shorr [9]. For the range from 1.5 to 0 mM 2,3-Pzglycerate the measurement was performed kinetically according to Bergmeyer [7].…”

Section: Determination Of Metabolitesmentioning

confidence: 99%

pH‐Dependent Changes of 2,3‐Bisphosphoglycerate in Human Red Cells during Transitional and Steady States in vitro

Rapoport

Berger

Elsner

et al. 1977

European Journal of Biochemistry

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A systematic study of the pH-dependent changes in the range 6.6 -7.4 of 2,3-bisphosphoglycerate and the adenine nucleotides was performed in the presence and absence of glucose during transitional and steady states.1. The results indicate that 2,3-bisphosphoglycerate phosphatase breaks down 2,3-bisphosphoglycerate nearly independent of pH at a rate of 480 pmol 2,3-bisphosphoglycerate x 1 cells-' x h-'. 2,3-Bisphosphoglycerate mutase is practically completely inhibited below pH 6.9. An increased K, 2,3-bisphosphoglycerate is postulated. The 2,3-bisphosphoglycerate level in the presence of glucose reaches a pH-dependent steady state after about 18 h in keeping with theoretical predictions.2. The constancy of the adenine nucleotides in the presence of glucose regardless of the rate of glycolysis indicates a close coupling between ATP formation and breakdown. The decline of the sum of adenine nucleotides appears to be determined by the rate of AMP breakdown.3. The share of the 2,3-bisphosphoglycerate bypass in the steady state decreases from 24% at pH 7.4 to 12 % at pH 7.04. The initially decreased glycolysis at low pH values increases in long-term experiments with lower 2,3-bisphosphoglycerate levels. The formation of pyruvate corresponds to the breakdown of 2,3-bisphosphoglycerate after consumption of an unknown reducing substance.The original observations of a breakdown of 2,3-P,glycerate [l -31 at low pH values, both in uivo and in vitro have been confirmed repeatedly. Nevertheless a systematic study of this phenomenon has not been performed so far, nor has its mechanism been elucidated. At present there is a lack of understanding by what mechanism steady state concentrations of 2,3-P,-glycerate are established under various physiological and pathological conditions. The experiments carried out so far in vitro do not permit valid extrapolations to the conditions in vivo. The purpose of the present study was an investigation of the pH-dependent kinetics of the changes of 2,3-P2glycerate both during transitional and steady states. It included an assessment of both the over-all flux through glycolysis as well as through the 2,3-P2glycerate bypass. In addition the behaviour of the adenine nucleotides was studied.Abbreviations. 2,3-P2glycerate, 2,3-bisphosphoglycerate; 1,3-Enzymes.

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A Simplified Method for Estimating Urinary Inorganic Phosphate during Aluminum Gel Therapy for Phosphatic Calculi

Cited by 44 publications

References 4 publications

Anticarcinogenic Activity of Allylmercaptocaptopril Against Aflatoxin-B1 Induced Liver Carcinoma in Rats

Anticarcinogenic Activity of Allylmercaptocaptopril Against Aflatoxin-B1 Induced Liver Carcinoma in Rats

Identification of the β _TP site in the x-ray structure of F ₁ -ATPase as the high-affinity catalytic site

pH‐Dependent Changes of 2,3‐Bisphosphoglycerate in Human Red Cells during Transitional and Steady States in vitro

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A Simplified Method for Estimating Urinary Inorganic Phosphate during Aluminum Gel Therapy for Phosphatic Calculi

Cited by 44 publications

References 4 publications

Anticarcinogenic Activity of Allylmercaptocaptopril Against Aflatoxin-B1 Induced Liver Carcinoma in Rats

Anticarcinogenic Activity of Allylmercaptocaptopril Against Aflatoxin-B1 Induced Liver Carcinoma in Rats

Identification of the β TP site in the x-ray structure of F 1 -ATPase as the high-affinity catalytic site

pH‐Dependent Changes of 2,3‐Bisphosphoglycerate in Human Red Cells during Transitional and Steady States in vitro

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Identification of the β _TP site in the x-ray structure of F ₁ -ATPase as the high-affinity catalytic site