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PubMed1975

Further studies on the binding of divalent cations to the phosphoglycoprotein phosvitin.

Dialysis equilibrium measurements at 25 degrees indicate that, at pH 6.8 and at a concentration of 1.0 times 10(-10) 3 M MnC12 or CoC12, phosvitin binds 113 Mn2+ and 120 Co2+. The binding is cooperative at low cation concentrations. The number of Mg2+, Ca2+, Mn2+, and Co2+ bound is not affected by temperatures of up to 60 degrees; however, the cooperactivity is enhanced. Optical rotatory dispersion and circular dichroism studies indicate that a conformational change occurs on binding of Mn2+ and Co2+ which parallels the one produced by Ca2+ and reported elsewhere [Grizzuti, K., and Perlmann, G.E. (1973), Biochemistry 12, 4399]. The conformational changes induced by Mg2+ and Mn2+ follow different paths. Upon binding of Mn2+ and Co2+ the intrinsic viscosity, [eta], of phosvitin decreases from about 0.5 to 0.03 dl/g, while Mg2+ and Ca2+ decrease [eta] to 0.048 dl/g. The ultraviolet absorption spectrum of phosvitin is altered upon binding of Ca2+, Mn2+, and Co2+, but not upon binding of Mg2+; an increase of the temperature to 60% has no further effect on the spectra.

Binding Sites↗
PubMed2001

Phalloidin affects the myosin-dependent sliding velocities of actin filaments in a bound-divalent cation dependent manner.

We examined sliding velocities in vitro of four types of actin filaments, that is, filaments with Ca2+ or Mg2+ bound at the high affinity metal binding site, each with rhodamine phalloidin bound with a high or low stoichiometry. When surfaces coated with a high density of heavy meromyosin (HMM) were used, high stoichiometric concentrations of rhodamine phalloidin reduced sliding velocities of only Ca2+-actin filaments, by 40%. As the HMM density on surfaces was reduced, continuous movement of actin filaments became dependent on the presence of methylcellulose and sliding velocities of all four types became progressively slower. Interestingly, Ca2+-actin filaments with a high stoichiometric concentration of rhodamine phalloidin were the fastest among the four types of filaments on sparse HMM surfaces. In contrast, phalloidin did not affect steady state ATPase activities of HMM in the presence of Ca2+- or Mg2+-actin filaments. We speculate that the reversal of the order of sliding velocities among the four types of actin filaments between high and low densities of HMM relates with different axial elasticity of the actin filaments, so that stiffer filaments move slower on dense HMM surfaces, but faster on sparse surfaces, than elastic ones.

Actin Cytoskeleton↗
PubMed2001

Influence of divalent cations on the catalytic properties and secondary structure of unadenylylated glutamine synthetase from Azospirillum brasilense.

Fully unadenylylated glutamine synthetase (GS) from the endophytic bacterium Azospirillum brasilense Sp245 was isolated and purified. The enzyme was electrophoretically homogeneous and contained strongly bound metal ions, which could not be removed by dialysis. Mn2+, Mg2+, and Co2+ were found to be effective in supporting biosynthetic activity of the A. brasilense GS. Some kinetic properties of Mn2+-activated and Mg2+-activated unadenylylated GS were characterized. Circular dichroism analysis of the enzyme showed that the A. brasilense GS is a highly structured protein: 59% of its residues form alpha-helices and 13% beta-strands. Removal of the metal ions from the A. brasilense GS by treatment with EDTA resulted in alterations in the enzyme secondary structure.

Adenosine Monophosphate↗
PubMed1997

Characterization of [35S]-ATP alpha S and [3H]-alpha, beta-MeATP binding sites in rat brain cortical synaptosomes: regulation of ligand binding by divalent cations.

1. We made a comparative analysis of the binding characteristics of the radioligands [35S]-ATP alpha S and [3H]-alpha, beta-MeATP in order to test whether these ligands can be used to analyse P2-purinoceptors in synaptosomal membranes from rat brain cortex. 2. Synaptosomes possess sites with high affinity for [35S]-ATP alpha S (Kd = 22.2 +/- 9.1 nM, Bmax = 14.8 pmol mg-1 protein). The rank order of the competition potency of the different compounds (ATP alpha S, ATP, ATP gamma S > ADP beta S, 2-MeSATP > deoxyATP, ADP > > UTP, alpha, beta-MeATP, AMP, Reactive Blue-2, suramin, isoPPADS) is consistent with pharmacological properties of P2Y-purinoceptors. 3. Under identical conditions [35S]-ATP alpha S and [3H]-alpha, beta-MeATP bind to different binding sites at synaptosomal membranes from rat brain cortex. The affinity of the [3H]-alpha, beta-MeATP binding sites (Kd = 13.7 +/- 1.8 nM, Bmax = 6.34 +/- 0.28 pmol mg-1 protein) was 38 fold higher than the potency of alpha, beta-MeATP to displace [35S]-ATP alpha S binding (Ki = 0.52 microM). ATP and ADP beta S competed at both binding sites with different affinities, 60 fold and 175 fold, respectively. The other agonists tested (2-MeSATP, UTP, GTP) did not affect specific [35H]-alpha, beta-MeATP binding at concentrations up to 100 microM. The antagonists (suramin, isoPPADS, Evan's Blue) showed completely different affinities for both binding sites. 4. Binding of [35S]-ATP alpha S on synaptosomes was regulated by GTP, which is indicative for G-protein coupled receptors. The Kd value for the high affinity binding site was reduced in the presence of GTP about 5 fold (from 1.8 nM to 8.6 nM). In the presence of Mg2+ the affinity was increased (Kd 1.8 nM versus 22 nM in the absence of Mg2+). 5. The binding of both radioligands was regulated in an opposite manner by physiological concentrations of Ca2+ and Mg2+. Binding of [3H]-alpha, beta-MeATP to synaptosomal membranes was increased 3 fold by raising the Ca2+ concentration from 10 microM to 1 mM, whereas the addition of Mg2+ in the same concentration range resulted in an 80% reduction of the binding. In contrast, [35S]-ATP alpha S binding was not influenced at the same range of Ca2+ or Mg2+ concentrations (10 microM to 1 mM). The addition of Mg2+ (5 mM) increased the affinity of [35S]-ATP alpha S for the high affinity site 10 fold. 6. Diadenosine polyphosphates had a bimodal effect on [35S]-ATP alpha S binding to synaptosomal membranes. AP5A and Ap6A enhanced binding of [35S]-ATP alpha S 1.6 fold in a concentration range between 0.1 and 50 microM. Ap3A was a weak inhibitor with a Ki value of 7.2 microM. Ap4A, AP5A and Ap6A inhibited with Ki values > 100 microM. These data support the concept that diadenosine polyphosphates do not directly interact with ATP alpha S binding sites. 7. In conclusion, on the basis of present knowledge of the interaction of P2-purinoceptor active compounds with P2x- and/or P2Y-purinoceptors, our data strongly suggest that [35S]-ATP alpha S is a useful tool to study P2Y-purinoceptors. Thus, the [35S]-ATP alpha S binding site might to a large extent represent P2Y-purinoceptors in synaptosomes from rat brain cortex. The nucleotide binding is regulated by G proteins, indicated by the effects of GTP/Mg2+ on binding.

Adenosine Triphosphate↗
PubMed1999

Investigations on the role of cytochrome b5 and divalent cations in the maximal nifedipine oxidase activity of human liver.

Native human cytochrome P4503A4 was most active in nifedipine oxidation when incorporated into a binary phospholipid vesicular system with human NADPH-cytochrome P450 reductase. The turnover numbers were estimated to be 17.6 and 19.6 min-1 in the presence of Mg2+ or Ca2+ ions (5 mmol/l) in the test system, respectively. Inclusion of b5 in the vesicular CYP3A4: reductase system results in a slightly lower nifedipine oxidase activity of 16.9 min-1 in the presence of Mg2+ ions. These results demonstrate that b5 is not an essential component in CYP3A4 catalyzed nifedipine oxidation in human liver.

Amino Acid Sequence↗
PubMed1983

Divalent cations in essential hypertension. Relations between serum ionized calcium, magnesium, and plasma renin activity.

We studied the relation of plasma renin activity to serum levels of ionized calcium and magnesium in 102 normotensive patients and in 98 patients with essential hypertension who were divided into low-renin, normal-renin, and high-renin groups. Serum magnesium levels were higher in patients with low-renin hypertension and lower in patients with high-renin hypertension than in those with normal-renin hypertension (P less than 0.025 for both comparisons) or in normotensive controls (P less than 0.005, P less than 0.05, respectively). In contrast, serum levels of ionized calcium were lower in patients with low-renin hypertension and higher in patients with high-renin hypertension than in those with normal-renin hypertension (P less than 0.001, P less than 0.05, respectively) or in normotensive controls (P less than 0.001, P less than 0.05, respectively). Altogether, the range of plasma renin activity in essential hypertension shows a continuous negative correlation with the serum magnesium level (r = -0.60, P less than 0.001) and a positive correlation with the serum ionized calcium level (r = 0.44, P less than 0.001). Accordingly, plasma renin activity in hypertension may reflect or contribute to changes in calcium and magnesium fluxes across cell membranes.

Calcium↗
PubMed1988

Control of ram sperm adenylate cyclase by divalent cations.

The adenylate cyclase activity of ram sperm increased on freeze-thawing and the enzyme was stable at 0 degrees C. Its activity was stimulated by Mn2+, Zn2+, Co2+, Mg2+ and Ca2+ in descending order of activity. The enzyme was insensitive to fluoride when Mn2+ concentration was in excess. Mn2+-stimulated enzyme activity was decreased by the simultaneous addition of Co2+, or Cd2+, or Ni2+, and particularly Cu2+. Sulfhydryl compounds (viz. dithiothreitol, glutathione, dithiocarbamate, 2-mercaptoethanol, ergothioneine and cysteine) and chelating agents (viz. D-penicillamine and 8-hydroxyquinoline) were effective, to varying degrees, in overcoming the inhibition by Cu2+. Ca2+ augmented the stimulatory effect of Mg2+, Co2+, Zn2+ and Mn2+ on enzyme activity.

Adenylyl Cyclases↗
PubMed1984

Intracellular free magnesium in erythrocytes of essential hypertension: relation to blood pressure and serum divalent cations.

Intracellular levels of free Mg2+ in human erythrocytes were determined by 31P NMR spectroscopy in 26 fasted subjects and were correlated with blood pressures and serum levels of total magnesium (bound and free Mg2+) and ionized calcium from the same subjects in a seated position. Untreated hypertensive individuals consistently demonstrated lower levels of intracellular free magnesium (192 +/- 8 microM, n = 11) than either normotensive (261 +/- 9.8 microM, n = 7, P less than 0.001 vs. untreated hypertensive subjects) or hypertensive subjects whose blood pressure had been normalized on therapy (237 +/- 7.8 microM, n = 8, P less than 0.005 vs. untreated hypertensives). For all subjects, strong relationships existed between intracellular free magnesium and diastolic blood pressure (r = -0.85, P less than 0.001) and systolic blood pressure (r = -0.71, P less than 0.001). Significant relationships also were observed between intracellular free magnesium levels and extracellular serum levels of calcium ion (r = -0.77, P less than 0.001) as well as serum concentrations of total magnesium (r = 0.62, P less than 0.001). We conclude that significant depletion of intracellular free magnesium levels are apparent in erythrocytes of subjects with essential hypertension. Furthermore, the close, inverse relationship of free magnesium levels with the height of the blood pressure suggests that abnormalities of intracellular magnesium metabolism may contribute to the pathophysiology of human essential hypertension.

Blood Pressure↗