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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The recently-developed large zone difference profile method in scanning molecular sieve chromatography is applied to the analysis of the Gibbs-Duhem expression in the tetramer-dimer equilibrium of human oxyhemoglobin A. The preferential binding term and solvation parameters of the Hofmeister anion phosphate are examined. Results indicate that as the concentration of phosphate ions increase, a hydrated phosphate is formed which enhances the association by perturbing the solvation layer of the hemoglobin molecules. The standard free energy change at a given Hofmeister anion activity of ln Ax = -3.2476 is 9.4 +/- 0.2 kcal/mole. delta G0 at ln Ax = -1.2711 is 10.90 +/- 0.05 kcal/mole, suggesting that approximately 11 kcal are required to dissociate one mole of tetramer into dimer.
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PMID:Scanning molecular sieve chromatography of interacting protein systems. IV. The difference profile method as applied to the Gibbs-Duhem expression in the analysis of the dimer-tetramer equilibria of oxyhemoglobin A. 46 45

The temperature and concentration dependent association of beta-casein was studied by means of viscometry, gel filtration chromatography, electron microscopy, analytical ultracentrifugation and UV difference spectrophotometry. Degrees of polymerization of 12, 22 and 49 and free energies of association of -21, -23 and -25kJ/mole monomer were found at temperatures of 10, 15 and 20 degrees C respectively in 0.2 M Na phosphate buffer pH 6.7. Monomeric beta-casein was not a completely random coil but became more compact with increasing temperature, due to hydrophobic interactions.
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PMID:Structure of beta-casein. 46 56

An enzyme that catalyzes the conversion of 2-amino-6-(5'-triphosphoribosyl)amino-5- or 6-formamido-6-hydroxypyrimidine, but not of guanosine triphosphate, to quinonoid 6-(D-erythro-1'-2'-3'-trihydroxypropyl)dihydropterin triphosphate and formic acid has been purified to homogeneity from some mammalian brain and liver. The enzyme of a single strand is a basic protein of 9177 daltons consisting of 68 amino acid residues--except the enzyme from rat brain, which has one additional aspartic acid as residue 7. The enzyme possesses three free SH groups and, in its most active form, 1 mol of phosphate per mole of enzyme. Peptides isolated after hydrolysis with trypsin, chymotrypsin, or weak acid were separated by thin-layer chromatography and sequenced manually by Edman degradation. The complete sequence of the molecule was established as follows: (formula: see text)
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PMID:Biopterin. VI. Purification and primary amino acid sequence of mammalian D-erythro-7,8-dihydroneopterin triphosphate synthetase. 49 48

Structural changes of chromatin induced by interaction of netropsin (Nt) with DNA has been examined by analysis of CD and electromicroscopic measurements. The results demonstrate the existence of a transition from the condensed globular state of chromatin into nucleosomal fibres generated by extremely low Nt concentration up to 1 mole Nt per 200 nucleotides. A second transition occurs at high Nt ratio per DNA phosphate (v' = 0.3). involving disorganization of nucleosomal particles. The interference of the Nt binding with chromatin proteins maintaining the sub- and superstructure will be discussed.
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PMID:Structural transitions of chromatin induced by netropsin. 51 94

1. The canine gastric arterial supply was isolated and perfused by means of an extracorporeal circuit. The gastric venous blood was returned to the dog's venous system. Histamine acid phosphate (20 microgram min-1) infused intra-arterially gave a mean peak acid output of 2.3 m-mole per 10 min. 2. When a plateau of acid secretion was observed, the gastric venous blood was diverted to the oxygenator, by-passing the dog entirely (vascular isolation). This resulted in an immediate decrease in acid output which fell to or near zero by 90 min after isolation. 3. In three dogs, part of a lung was perfused in series with the stomach before total isolation of the gastric vasculature. With histamine stimulation, acid secretion was observed for about 1 hr with a peak acid output of 0.5 m-mole per 10 min during the period of total isolation. 4. Indomethacin (10 mg kg-1) was given to five dogs approximately 1 hr before vascular isolation. After acid secretion reached a plateau (mean peak acid output 2.3 m-mole per 10 minutes), the gastric circulation was isolated by diverting the gastric venous blood to the oxygenator. Acid secretion was maintained for 50 min, after which it gradually declined to reach 30% of the peak value after 2 hr. 5. Indomethacin (10 mg kg-1) and methysergide bimaleate (1 mg) were given I.V. to five dogs approximately 1 hr before vascular isolation. After acid secretion reached a plateau (peak output 3.0 m-mole per 10 min), the gastric circulation was isolated by diverting the gastric venous blood to the oxygenator. The plateau of secretion was maintained for a further 2 hr with no inhibition. 6. Methysergide bimaleate given alone did not prevent the inhibition of secretion caused by the total vascular isolation of the stomach. 7. These results suggest that in the isolated canine stomach preparation naturally occurring inhibitors of gastric acid secretion, which are normally metabolized at least in part in the lungs, accumulate in the circulation and may account for the observed suppression of acid secretion.
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PMID:Acid secretion from the completely isolated blood perfused canine stomach. 52 72

A reduction in myocardial oxygen supply during ischemia, not only leads to reduced aerobic ATP production but does not stimulate glycolytic ATP synthesis. The residual aerobically synthesized ATP comes primarily from continued inefficient (i.e., compared to glucose in terms of moles of ATP produced per mole of O2 consumed) oxidation of fatty acids. This leads to elevated tissue levels of long chain fatty acyl-CoA and fatty acyl-carnitine. Both are potentially cell damaging metabolic intermediates. Restriction of glycolysis is due to inhibition of glyceraldehyde-3-phosphate dehydrogenase by accumulated metabolites, such as H+, lactate and NADH. The reduced production of ATP leads to decreased levels of high energy phosphate stores which in turn may impair myocardial mechanical function.
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PMID:Energy metabolism in the ischemic heart. 55 21

Radioactively labeled tubulin from Chinese hamster ovary (CHO) cells can be isolated by co-polymerization with nonradioactive porcine brain microtubule protein. 75% of the soluble tubulin in CHO extracts co-polymerizes with the porcine protein through several cycles, without preferential loss of either CHO or porcine subunits. After phosphocellulose chromatography of the co-polymerized microtubules, the CHO tubulin is radiochemically homogeneous, as judged by SDS-polyacrylamide gel electrophoresis. CHO tubulin purified in this way has 1 mole of nucleotide per mole of protein noncovalently bound at the non-exchangeable or N site. This-layer chromatography indicates that the N site nucleotide is entirely ribo-GTP. Label and chase experiments show that the N site GTP exchanges intracellularly with a half-time of 33 hr in growing cells which have a generation time of 17 hr, while the tubulin polypeptides are degraded with a half-time of 48 hr. Intracellular hydrolysis of the gamma-phosphate of the N site nucleotide can be detected but occurs very slowly, with a half-time of 24 hr. These results suggest that the N site nucleotide may function in vivo as a stable structural co-factor of the tubulin molecule and render improbable the possibility that it has a regulatory role in microtubule assembly.
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PMID:Turnover of tubulin and the N site GTP in Chinese hamster ovary cells. 56 16

The ability of succinyl-CoA-synthetase from pigeon thoracic muscle to interact with ATP is investigated. gamma-32P-ATP and 8-14C-ATP were used in experiments. It is found that the enzyme, when reacting with ATP in the presence of Mg2+, forms a complex containing 2 moles of ATP residue and 2 moles of phosphoric acid residue (splitted from ATP) per 1 mole of protein. After 2 hours of incubation at 0-4 degrees C, the complex is converted into another one, containing 4 residues of phosphoric acid per 1 mole of @protein. Both complexes are active, and their incubation with succinate and CoA results in the formation of succinyl-CoA. The reaction capacity of these enzyme complexes with some reaction substrates is investigated. The enzyme complex containing 2 phosphoric acid residues and 2 nucleotide residues is found to interact neither with CoA, nor with succinate. The enzyme complex containing 4 phosphoric acid residues does not react with CoA, but it interacts with 14C-succinate, releasing inorganic phosphate in the amount equivalent to the equimolar amount of protein-binding succinic acid.
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PMID:[Reaction mechanism of succinyl CoA synthetase from pigeon thoracic muscle]. 57 66

With radioactive compounds of high specific activity, the binding of carcinogens to DNA can be measured with doses that are ineffective in long-term studies. The binding of tritiated benzo(a)pyrene to liver DNA of adult male rats has been determined 50 hr after a single i.p. injection of doses between 40 microgram/kg and 4 mg/kg. The dose-response relationship is linear up to 1 mg/kg, shows a step towards 2 mg/kg, and gives a shallow linear slope above that value. The observed binding ranges from 1.7 to 180 nmoles benzo(a)pyrene per mole DNA phosphate. The nonlinearity could be due to an induction of metabolizing enzymes. The microsomal aryl hydrocarbon hydroxylase activity increases significantly 24 hr after a single dose of 4 mg/kg and 48 hr after doses of 2 and 4 mg/kg, but no induction is found with 1 mg/kg. The binding from an equimolar dose is 35 times lower than the one found on mouse skin DNA and 300 times lower than that of N,N-dimethylnitrosamine in rat liver. A good correlation exists to the respective tumor formation in long-term studies.
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PMID:Nonlinear dose-response relationship for the binding of the carcinogen benzo(a)pyrene to rat liver DNA in vivo. 62 63

The M-line protein component of molecular weight 165 000 was isolated and purified from rabbit skeletal muscle using ion exchange chromatography. Gel electrophoresis, in the presence and absence of sodium dodecyl sulfate, revealed the protein to be homogeneous. Sodium dodecyl sulfate gel electrophoresis and low speed sedimentation equilibrium studies in 0.5 M KCl, 50 mM potassium phosphate gave a molecular weight of 165 000 suggesting the protein to be made up of a single polypeptide chain. Circular dichroism spectra revealed the presence of two negative dichroic bands located at 216 and 208 nm, indicative of the presence of some beta-structure. Ellipticity values at these two wavelengths were --6500 +/- 400 and --7500 +/- 400 deg . cm2 . dmol-1, respectively. Addition of 165 000 component lowered the enzymatic activity of creatine kinase M-line protein and the nature of the inhibition was found to be a competitive one. When the protein was mixed with creatine kinase in a 1 : 1 mole ratio in a medium consisting of 0.2 M KCl, 25 mM Tris, 1 mM dithiothreitol (pH 8.0), low speed sedimentation equilibrium studies gave a molecular weight of 260 000 +/- 10 000 for the complex, indicative of an interaction of the two components of the M-line.
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PMID:Isolation and characterization of the 165 000 dalton protein component of the M-line of rabbit skeletal muscle and its interaction with creatine kinase. 63 91


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