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Query: UMLS:C0027960 (mole)
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Pyruvate kinase (EC 2.7.1.40) of S. carlsbergensis is a tetrameric enzyme, composed of four identical subunits each of which contains 1 mole of L-valine noncovalently bound. The enzyme readily dissociates into monomeric units. L-Valine and magnesium or manganese ions are specific primers of the renaturation process of the enzyme. The amino acid induces renaturation with a K(0.5) of 17 muM and a pseudo first-order rate constant of 0.019 min(-1) at 25 degrees with respect to the monomeric species, indicating that L-valine influences the folding of the monomeric form from a disordered state to its native conformation being followed by a spontaneous reassociation with formation of the tetrameric enzyme. Independently, magnesium and manganese ions induce the renaturation with a first-order rate constant of the same magnitude.
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PMID:Mechanism of renaturation of pyruvate kinase of Saccharomyces carlsbergensis: activation by L-valine and magnesium and manganese ions. 452 55

A thermostable beta-galactosidase (EC 3.2.1.23; beta-dgalactoside galactohydrolase) was found to be inducible in an extreme thermophile resembling Thermus aquaticus. Enzyme induction was achieved by the addition of lactose, galactose, or the alpha-galactoside, melibiose, to growing cultures. The addition of glucose to induced cultures had a repressive effect on further enzyme synthesis. The enzyme was purified 78-fold, and the optimum temperature and pH for activity were determined to be 80 C and pH 5.0, respectively. The enzyme was activated by both manganese and ferrous iron. Sulfhydryl activation and thermal stabilization indicate that the thermophilic beta-galactosidase is a sulfhydryl enzyme. Kinetic determinations at 80 C established a K(m) of 2.0 x 10(-3)m for the chromogenic substrate o-nitrophenyl beta-d-galactopyranoside (ONPG) and a K(1) of 7.5 x 10(-3)m for lactose. The Arrhenius energy of activation (for the hydrolysis of ONPG) was calculated to be 13.7 kcal/mole. A molecular weight of 5.7 x 10(5) daltons was estimated by elution of the enzyme from Sephadex 4B.
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PMID:Induction and characterization of -galactosidase in an extreme thermophile. 502 73

1. Changes in ionized calcium in giant axons were followed by recording the light produced by injected aequorin.2. From the effect of injecting calcium buffers the internal concentration of ionized calcium was found to be about the same as in a mixture of 45 Ca EGTA:55 free EGTA, i.e. about 0.3 muM.3. After an axon had been exposed to cyanide for 50-100 min the velocity of the aequorin reaction increased about 500 times. This effect, which could be reversed rapidly by removing cyanide, was probably brought about by release of calcium from an internal store.4. Injecting 30 mumole ATP per litre of axoplasm into a cyanide-poisoned axon caused a transient lowering of light intensity; oligomycin blocked the effect.5. Raising external calcium or replacing external sodium by choline or lithium reversibly increased the light produced by axons injected with aequorin.6. Stimulation at 50-200 impulses/sec in a solution containing 112 mM-Ca caused the light intensity to increase to a new steady level; after stimulation the light intensity returned to its original level with a time constant of 10-30 sec. Similar but smaller effects were seen in solutions containing less external calcium. The recovery after stimulation is probably due to uptake of calcium by the internal store.7. Injecting 3 m-mole EGTA per litre axoplasm lowered the resting glow and abolished the aequorin response to stimulation.8. There was no light response to stimulation immediately after an axial injection of aequorin and the effect increased to a ;steady' level with a half-time of about 5 min. The conclusion is that the rise in calcium concentration resulting from stimulation is confined to the peripheral part of the axon and that the diffusion coefficient of aequorin in axoplasm is about 4 x 10(-7) cm(2)/sec.9. The increment in light per impulse often increased markedly during the course of a long experiment and there was also considerable variation between axons.10. If the light response to stimulation was small it was proportional to the frequency of stimulation; if large to the square of the frequency.11. Voltage-clamp experiments showed that the calcium entry associated with a depolarizing pulse could be divided into an early component which was abolished by tetrodotoxin (TTX), and a late component which was unaffected by this inhibitor.12. The time relations of the early calcium entry were consistent with its being a leak of calcium ions through the sodium channel; the permeability of the sodium channel to calcium was about 1% of the permeability to sodium.13. The late entry of calcium was little changed by injecting enough tetraethylammonium (TEA) to block the outward potassium current; it was greatly reduced by external concentrations of manganese which had little effect on the maximum potassium conductance.14. The voltage-response curve for the late entry of calcium had a well defined maximum and was similar in shape to the curve relating calcium entry to depolarization at the presynaptic ending (Katz & Miledi, 1969, 1970).
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PMID:Depolarization and calcium entry in squid giant axons. 513 53

Nicotinamide adenine dinucleotide phosphate-specific isocitrate dehydrogenase was extracted from etiolated pea (Pisum sativum L.) seedlings and was purified 65-fold. The purified enzyme exhibits one predominant protein band by polyacrylamide gel electrophoresis, which corresponds to the dehydrogenase activity as measured by the nitro blue tetrazolium technique. The reaction is readily reversible, the pH optima for the forward (nicotinamide adenine dinucleotide phosphate reduction) and reverse reactions being 8.4 and 6.0, respectively. The enzyme has different cofactor and inhibitor characteristics in the two directions. Manganese ions can be used as a cofactor for the reaction in each direction but magnesium ions only act as a cofactor in the forward reaction. Zinc ions, and to a lesser extent calcium ions, inhibit the enzyme at low concentrations when magnesium but not manganese is the metal activator. It is suggested that there is a fundamental difference between magnesium and manganese in the activation of the enzyme. The enzyme shows normal kinetics and the Michaelis contant for each substrate was determined. The inhibition by nucleotides, nucleosides, reaction products, and related compounds was studied. The enzyme shows a linear response to the mole fraction of reduced nicotinamide adenine dinucleotide phosphate when total nicotinamide adenine dinucleotide phosphate (nicotinamide adenine dinucleotide phosphate plus reduced nicotinamide adenine dinucleotide phosphate) is kept constant. Isocitrate in the presence of divalent metal ions will protect the enzyme from inactivation by p-chloromercuribenzoate. Protection is also afforded by manganese ions alone but not by magnesium ions alone There is a concerted inhibition of the enzyme by oxalacetate and glyoxylate.
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PMID:Nicotinamide adenine dinucleotide phosphate-specific isocitrate dehydrogenase from a higher plant. Isolation and charactertization. 554 83

The activation of ovine brain glutamine synthetase by Mn(II) or Mg(II) was studied by steady-state kinetics. The metal ion concentration was varied at several fixed concentrations of ATP, and vice versa, and the resultant kinetic curves were analyzed according to the method of London and Steck [London, W. P., & Steck, T. L. (1969) Biochemistry 8, 1767-1779]. The data for Mg(II) indicated optimal activation at Mg:ATP = 2:1, whereas that for Mn(II) occurred at Mn:ATP = 1:1. This was interpreted as indicating formation of Mg . E . Mg . ATP as the subunit complex of optimum activity with Mg(II) (pHopt 7.5). With Mn(II) (pHopt 5.0), the complex of optimum activity may be either E . Mn . ATP or Mn . E . Mn . ATP, where the Mn . E complex is very tight. So that the latter two possibilities could be distinguished, titrations of the enzyme with Mn(II) were performed, electron paramagnetic resonance being used to determine free Mn(II). Four moles of Mn(II) ions was found to bind per mole of octameric enzyme, with an apparent Kd congruent to 0.54 microM. Addition of either HCl or Nd(III) ions to Chelex-treated enzyme results in the release of 3.7 +/- 0.2 Mn(II) ions. Thus, it appears that four Mn(II) are very tightly bound per octamer and that four more Mn(II) can bind tightly. Neither Mg(II) nor Ca(II) at 50 mM can displace Mn(II) from the Mn4 . E complex, but Mn(II) still binds tightly to apoenzyme or Mn4E in the presence of 50 mM Mg(II). As one proceeds from apo-E to Mn4 . E to Mn4 . E . Mn4 (+/- ATP), the intensity of the fluorescence emission of protein tryptophan residues decreases strongly and successively. The specific activities of the apo-E, Mn4 . E, and Mn4 . E . Mn4 complexes were found to be 0, 50, and 200 units/mg, respectively. If apoenzyme is added to a continuous coupled assay system with Mg(II), buffer, and with or without Mn(II) present, a time-dependent activation is observable with t1/2 congruent to 0.5-1.0 min. The total intracellular concentration of Mn(II) in ovine brain tissue was determined to be 1.9-2.6 microM, whereas the free [Mn(II)] was below 0.5 microM. Since the enzyme binds Mn(II) in preference to other divalent ions, it appears that the enzyme may exist as a manganoenzyme in vivo.
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PMID:Glutamine synthetase from ovine brain is a manganese(II) enzyme. 612 92

The kinetic properties of glutamine synthetase (EC 6.3.1.2) isolated from pea chloroplasts and purified according to the previously developed procedure have been investigated. The pH optimum for the enzymatic reaction in the presence of Mg2+ and Mn2+ are 7.5-7.6 and 5.5, respectively. The corresponding values of the activation energy per enzyme monomer (Mr = 60 000) are equal to 2900 and 1190 cal/mole. With Mg2+ the values of Km(app.) for NH4+, NH2OH, L-glutamate (+NH4+), L-glutamate (+NH2OH), ATP(+NH4+ and NH2OH) and Mg-ATP (+NH4+ and NH2OH) are 0.64, 17.5, 5.6, 7.0, 1.3 and 0.74 mM, respectively.
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PMID:[Kinetic characteristics of glutamine synthetase from the chloroplasts of pea leaves]. 613 4

A protein has been isolated from calf heart inner mitochondrial membrane with the aid of an electron paramagnetic resonance (EPR) assay based on the relative binding properties of Ca2+, Mn2+, and Mg2+ to the protein. The molecular weight of this protein has been estimated to be about 3000 by urea/sodium dodecyl sulfate-gel electrophoresis and amino acid analysis. The isolated protein has been shown to have high affinity and high specificity for Ca2+ (Jeng, A. Y., Ryan T. E., and Shamoo, A. E. (1978) Proc. Natl. Acad. Sci. U. S. A. 75, 2125-2129). However, the protein was found to be contaminated with a large amount of phospholipids. There are 150 mol of phospholipids associated with each mole of the protein. The protein is delipidated using Sephadex LH-20 column chromatography. The contaminating phospholipids can be reduced to 0.1 mol of phospholipids/mol of protein. There are no detectable free fatty acids, hexosamines, or sialic acids associated with the delipidated protein. This protein is named "calciphorin," meaning calcium ionophore protein.
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PMID:Isolation of a Ca2+ carrier from calf heart inner mitochondrial membrane. 624 37

A photoaffinity analogue of UDP-galactose, 4-azido-2-nitrophenyluridylyl pyrophosphate (ANUP), has been synthesized for the investigation of the binding topography of alpha-lactalbumin on galactosyltransferase. Results obtained from steady state kinetics show that ANUP is an effective competitive inhibitor against UDP-galactose in the reactions of lactose and N-acetyllactosamine syntheses. The specific binding of ANUP to the UDP-galactose-binding site is further demonstrated by its ability to facilitate the formation of the lactose synthase complex on solid supports, either alone or in the presence of glucose or N-acetyl-glucosamine. ANUP inactivates galactosyltransferase on irradiation. One mole of ANUP was incorporated per mol of enzyme inactivated. This process is Mn2+-dependent and can be prevented by UDP-galactose. Glucose and N-acetylglucosamine render only partial protection. Photoaffinity labeling of lactose synthase either free in solution or immobilized on Sepharose does not result in any reduction of the alpha-lactalbumin modifier activity. In addition, no incorporation of radioactivity into alpha-lactalbumin was observed when radioactive ANUP was used, whereas galactosyltransferase was labeled. These data indicate that alpha-lactalbumin does not bind to galactosyltransferase in the region of the ANUP site, suggesting that the location of protein-protein interaction between the two subunits of lactose synthase may be removed from the UDP-galactose-binding domain.
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PMID:Photoaffinity labeling of lactose synthase with a UDP-galactose analogue. 641 60

Extremely large separation factors (greater than 10(2)) were found for Na-Mg, K-Ca and Rb-Sr metal ion pairs on a cryptomelane-type hydrous manganese dioxide (CRYMO) ion exchanger. Ca2+ and Sr2+ ions were quantitatively separated from a thousand times of K+ and Rb+ ions on mole basis, respectively, by using the CRYMO column. The hopeful utilities of the CRYMO are suggested for the radiochemical ion-exchange separation of radiomagnesium and radiostrontium from K and Rb salt targets.
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PMID:Separation of trace amounts of Ca2+ and Sr2+ from K+ and Rb+ with a hydrous manganese dioxide ion exchanger. 647 37

Epidemiological investigations carried out on workers in certain areas of nickel refineries have shown that a relationship exists between exposure to certain nickel compounds and cancer of the nasal passages and the lungs. Animal experiments have shown that nickel compounds cause tumours, the carcinogenicity being greater the lower the solubility of the compound in water (solubility less than 10(-3) mole/l). Amorphous nickel monosulfide (solubility less than 10(-5) mole/l) is an exception to this rule. It has been demonstrated by X-ray photoelectron spectroscopy that the surface properties of crystalline nickel monosulfide differ from those of the amorphous variety, in that amorphous nickel monosulfide has a positive surface charge while that of the crystalline sulfide is negative. It would seem that, as in the case of asbestos, a negative surface charge is an important factor in the ability to transform cells. Carcinogens are electrophiles. The differences in the behaviour of nickel compounds can be explained by the theory of hard and soft acids and bases. These considerations and the differences in the rates of cell transformation show the importance of the methods used to prepare the compounds (precipitation from solution, reaction between the elements in vacuo, solid-gas reactions) which very often lead to the formation of non-stoichiometric phases (hexagonal nickel monosulfide, nickel monoxide, high-temperature nickel subsulfide) having completely different thermodynamic, electrical, magnetic and surface properties and specific surface areas. Phase and Eh pH diagrams as well as those of Ellingham (1948) for the nickel oxides and sulfides show that certain phases are unstable and that it is important to specify precisely the conditions governing storage, grinding, handling and injection. A precise knowledge is required of the chemical composition of ores, mattes and dusts, since certain elements and compounds, e.g., manganese, even when present only in trace amounts, can act either as promoters or inhibitors in biological processes. This paper therefore demonstrates the importance of specifying the methods of preparation and determining the physico-chemical properties and purity of nickel compounds before biological studies are undertaken.
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PMID:Influence of physicochemical properties, methods of preparation and purity of nickel compounds on their biological effects. 653 81


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