Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

It is well known that minerals of bone or tooth are essentially of CaO-P2O5 system. Glass and the crystallized product, i.e., so-called "glass-ceramics" of which chemical composition is 55 CaO . 45 P2O5 (in mole %) and have been developed for biomaterials were subjected to chemical durability test. Human enamel was also tested for the comparison of the data with them. All the specimens were ground to powders in size from 74 to 140 micrometer. A hundred milligram of the powders were immersed into 100 ml. of N/10 acetate buffer (1 mol acetic acid) solution (pH 4.1) at a constant temperature of 37 degrees C. Amount of Ca2+ and P5+ dissolved were determined by an atomic absorption method and Fiske-Subbarow method, respectively. The order of dissolution is human enamel greater than glass greater than glass-ceramics: the amount of Ca2+ (SCa) and P5+ (Sp) with soaking time (t) was expressed by the following equations, :formula: (see book). The glass and the glass-ceramics show good resistance against a weak acid.
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PMID:[Studies of calcium phosphate glass-ceramics--development of dental materials. (Part 2) Acid resistance--(author's transl)]. 28 65

Mentally handicapped children, aged 5--15 years and living in institutions, received fluoride supplement in several sugar products of their diet; in candies, marmalades, jams, fruit juices and in sweet desserts corresponding to 10 mg F as NaF per kg of the sugar (sucrose or glucose) of each product. To two of the four daily candies was also added a NaHCO3 + KH2PO4 mixture (mole ratio 9.8/l, resp.) to substitute for 2.5% of the sugar of the candy. The control children received the respective products without the additives. After stepwise exclusions of subjects for various reasons, e.g. for the absence of permanent teeth, low initial caries activity, strong medication, Down's syndrome, etc., the mean DMFS-increment in the remaining 43 control subjects was 4.5 and in the 41 test subjects 2.6 lesions/100 surfaces at risk, i.e. 42% reduction. Caries arrestment had occurred in these test subjects after the first year, while in the respective controls it was continuously increasing. Among numerous oral and body parameters studied, only surface enamel fluoride in primary teeth was increased by the fluoride supplements and urinary phosphate and calcium excretion decreased.
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PMID:Effect of caries in mentally handicapped children of addition of fluoride and bicarbonate-phosphate to dietary sugar products. 39 99

1. By a procedure involving adsorption to barium sulfate, chromatography on DEAE-Sephadex and QAE-Sephadex and preparative polyacrylamide gel electrophoresis, decarboxyfactor X was purified from plasma of phenprocoumon-treated cows. No contaminants could be detected in the final preparation by polyacrylamide gel electrophoresis and zone-electrophoresis. 2. The molecular weight of decarboxyfactor X, as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis is approximately 55 000, which is equal to that of factor X. The protein consists of two polypeptide chains with molecular weights of 44 000 and 17 000. 3. Decarboxyfactor X has antigenic determinants in common with normal factor X. 4. The amino acid composition and aminoterminal amino acids of normal factor X and decarboxyfactor X are identical. 5. Less than one residue of gamma-carboxyglutamate could be detected per mole of decarboxyfactor X. 6. In the absence of Ca2+, normal factor X has a slightly higher electrophoretic mobility than decarboxyfactor X. In the presence of Ca2+ the mobility of factor X decreases considerably while the mobility of decarboxyfactor X remains unaltered.
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PMID:Purification and properties of the phenprocoumon-induced decarboxyfactor X from bovine plasma. A comparison to normal factor X. 41 33

Factor V and factor Va binding to single bilayer phospholipid vesicles was investigated by light-scattering intensity measurements. This technique allows the measurement of free and phospholipid-bound protein concentrations from which equilibrium constants can be obtained. As controls, the Ca2+-dependent phospholipid binding of prothrombin and factor X were also studied. The average values obtained for the dissociation constants (Kd) and lipid to protein ratio at saturation, moles/mole (n), for prothrombin (Kd = 2.3 X 10(-6) M, n = 104) and factor X (Kd = 2.5 X 10(-6) M, n = 46) binding to vesicles containing 25% Folch fraction III and 75% phosphatidylcholine in the presence of 2 mM Ca2+ were in agreement with those reported in the literature. The average factor V and factor Va values for the dissociation constants and lipid to protein ratio at saturation (moles/mole) were Kd = 7.2 X 10(-8) M and n = 270 for factor V and Kd = 4.4 X 10(-7) M and n = 76 for factor Va. In contrast to prothrombin and factor X, factor V and factor Va demonstrated Ca2+-independent lipid binding. In addition, the number of factor V and factor Va molecules bound per vesicle was found to be dependent both on the phosphatidylserine content of the vesicle and the ionic strength of the buffer.
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PMID:Phospholipid-binding properties of bovine factor V and factor Va. 48 30

1. The influx of [3H]gamma-aminobutyric acid ([3H]GABA) into isolated rat superior cervical ganglia has been measured by radioassay, supplemented by autoradiography. Ganglia were incubated in oxygenated Krebs solution at 25 degrees C, containing 10 microM-amino-oxyacetic acid. Under these conditions more than 95% of accumulated tritium was unmetabolized [3H]GABA. 2. Ganglionic radioactivity increased linearly with incubation time, to yield an intracellular fluid/extracellular fluid concentration ratio (Ci/Co) of about 200 after 6 hr in 0.5 microM-external [3H]GABA. 3. Uptake showed saturation with an apparent transport constant (KT) of 6.8 microM and maximum influx velocity (Jmaxi) of 7 mumole 1. cell fluid-1- min-1. 4. The influx rate at Co = 0.5 microM was unaltered by raising intracellular GABA from 0.2 to 1 mM. 5. Influx velocity increased with temperature (5--35 degrees C) in a monotonic manner with an apparent activation energy of 14 kcal mole-1. 6. Concentrative uptake was depressed by reducing external [Na+] with ouabain, by raising [K+]o above 20 mM, or by removing external Cl-. Uptake was not particularly sensitive to Ca2+ or Mg2+ ions. 7. Utake of [3H]GABA (0.5 microM) was inhibited by beta-guanidinopropionic acid (apparent KI, 28 microM), beta-alanine (KI, 55 microM), gamma-amino-beta-hydroxybutyric acid (KI, 220 microM), beta-amino-n-butyric acid (KI, 708 microM), 3-aminopropanesulphonic acid (KI, 832 microM) and taurine (KI greater than 1 mM). Uptake was not depressed by 1 mM-glycine, alpha-alanine, leucine, serine, methionine or alpha-amino-iso-butyric acid. 8. Radioactively labelled methionine, leucine, glycine, serine, beta-alanine and taurine (concentrations less than or equal to 5 microM) were also taken up by ganglia. Of these, only uptake of beta-alanine and taurine were significantly depressed by 1 mM-GABA. 9. Autoradiographs confirmed that [3H]GABA and [3H] beta-alanine were taken up predominantly into extraneuronal sites (presumed to be neuroglial cells). Methionine, leucine, glycine and serine showed preferential accumulation in neurones. Neuronal uptake of leucine was not prevented by inhibiting protein synthesis. 10. Calculations of net fluxes from unidirectional tracer fluxes suggest that the sympathetic glial cells are capable of promoting net uptake of GABA at external concentrations above 1 microM.
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PMID:[3H]gamma-Aminobutyric acid uptake into neuroglial cells of rat superior cervical sympathetic ganglia. 50 28

The interaction of hematoporphyrin IX and two synthetic porphyrin tumor localizers, meso-tetra (4-carboxyphenyl) porphine (TCPP) and mesotetra (4-sulfonatophenyl) porphine (TPPS4) with fibrinogen was investigated in the presence and absence of light. Both TPPS4 and TCPP were found to bind to fibrinogen in greater than a 1/1 mole ratio in the absence of light. Chromatographic analysis indicated that during illumination TPP4 bound to fibrinogen to a greater extent that did either TCPP or hematoporphyrin. Both TCPP and TPPS4 were found to exhibit a greater inhibitory effect on clotting in the presence of light than did hematoporphyrin. In the absence of light and added Ca2+, both TCPP and TPPS4 were found to stimulate clotting at very specific porphyrin/fibrinogen concentration ratios, with TPPS4 being the more potent stimulator of the two. Hematoporphyrin exhibited little or no effect on clotting times. Fibrinogen, photoirradiated in the presence of the porphyrins was found to inhibit the clotting of unirradiated fibrinogen. A comparison of the stimulatory effects on clotting times by either calcium or TCPP and TPPS4 indicated that the porphyrins were capable of eliciting a greater stimulatory response than did calcium. The magnitude of the stimulatory response caused by the porphyrins alone was substantially reduced in the presence of calcium although the overall stimulatory response was increased but not additive. This suggests some interaction between either the calcium and porphyrin molecules or similarities in the respective stimulatory mechanism(s) involved. A possible correlation between these observations and the porphyrins ability to localize in tumors is also discussed.
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PMID:The effect of tumor localizing porphyrins on the conversion of fibrinogen to fibrin. 52 77

The urinary excretion of calcium, magnesium, oxalate, creatinine, phosphate and urate was investigated in patients with urolithiasis and in normal subjects. The excretion of oxalate and urate per mole creatinine and the quotients calcium/magnesium, calcium X oxalate/magnesium and calcium X oxalate/(magnesium X creatinine) were significantly higher in stone formers than in normal subjects. The mean creatinine-correlated urinary excretion of calcium was higher and of magnesium lower in patients with urolithiasis, but the differences were statistically not significant. The urine investigation was supplemented with analysis of calcium, magnesium, creatinine, urate, bicarbonate and chloride in serum and a qualitative analysis of stone composition. A simple schedule for a biochemical grouping of patients with urolithiasis is presented and on the basis of the analytical findings it was possible to classify 67% of patients with so-called 'idiopathic stone disease' according to these principles.
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PMID:A biochemical basis for grouping of patients with urolithiasis. 66 34

The binding of Ca+2 to bovine factor X (molecular weight of 74,000) (Yue und Gertler 1977) was studied by the technique of rate dialysis and with the use of 45Ca+2. The binding data are consistent with a model of sequential mechanism. One mole of Ca+2 binds to the glycoprotein with a dissociation constant of 5.2 X 10(-5) M and additional 39 +/- 4 moles of Ca+2 bind to this zymogen with a dissociation constant of 3.7 X 10(-3) M. The binding of the high affinity Ca+2 causes a functionally significant change in the zymogen, and (calcium) (factor X) complex is the real substrate in the activation process by the protease in Russell's viper venom.
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PMID:The binding of calcium ions to bovine factor X by rate dialysis. 73 34

1. Fluxes of 45Ca2+ were studied in pancreatic islets from non-inbred ob/ob-mice. Because La3+ blocked the transmembrane fluxes of 45Ca2+ in islet cells, incubations aimed at measuring glucose-induced changes of the intracellular Ca2+ were ended by washing the islets with 2 mM-La3+ for 60 min. 2. Uptake of 45Ca2+ progressed for 2 hr; the intracellular concentration of exchangable Ca2+ was about 7 m-mole/kg dry wt., as estimated from the isotope distribution at apparent equilibrium in islets exposed to 3 mM D-glucose. Raising the D-glucose concentration to 20 mM enhanced the 45 Ca2+ uptake whether or not the islets had first been equilibrated with the isotope. The stimulatory effect of D-glucose was observed in Tris buffer containing no anions but Cl- as well as in polyanionic bicarbonate buffer. The effect could not be reproduced with equimolar L-glucose. 3. The rate of 45Ca2+ release was the same whether the islets had been pre-loaded in the presence of 3 or 20 mM D-glucose. Thus the 45Ca2+ that had been taken up in response to 20 mM D-glucose appeared to be released much more slowly than the bulk of intracellular 45Ca2+. The release of 45Ca2+ was not significantly influenced by D-glucose during the release period. Incubation for 30 min was require for half of the radioactivity to be released. 4. The rates of insulin secretion were about the same in uni-anionic Tris buffer as in polyanionic bicarbonate buffer. A marked insulin secretory response to 20 mM D-glucose was observed in either buffer. 5. It is concluded that 20 mM D-glucose causes a net uptake of Ca2+ from the extracellular fluid into the interior of the beta-cells. This uptake is probably not regulated at the level of the plasma membrane but more likely reflects an increased affinity of some intracellular phase or compartment for the ion. Because the observed uptake and release of intracellular 45Ca2+ are slow processes in comparison with the rapid effects of extracellular Ca2+ on insulin secretion, insulin secretion may also depend on a more superficial and La3+-displacable Ca2+ pool.
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PMID:Effects of glucose on 45Ca2+ uptake by pancreatic islets as studied with the lanthanum method. 76 50

The M-line protein which is identical to the muscle form of creatine kinase was 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 gave 44 000 +/- 2000 as the minimum molecular weight while low speed sedimentation equilibrium experiments yielded a molecular weight of 84 000 +/- 4000, suggesting that the parent molecule is a dimer. Circular dichroism spectra revealed the presence of two negative dichroic bands located at 218 and 208 nm suggesting the presence of some beta-structure. Ellipticity values at these two wavelengths were -8000 +/- 400 and -9000 +/- 400 deg-cm2-dmol-1. Circular dichroism measurements indicated the protein to interact with myosin, heavy meromyosin and heavy meromyosin subfragment 1 (S1). The Ca2+-activated ATPase activities of myosin, heavy meromyosin and subfragment 1 were inhibited by the addition of M-line protein. When the protein was mixed with subfragment 1 in a 1:1 mole ratio in 0.15 M KC1, 50 mM Tris pH 8, low speed sedimentation equilibrium studies gave a molecular weight of 205 000 +/- 10 000 for the complex, indicative of an interaction of the two components. Both circular dichroism and sedimentation equilibrium studies indicated no interaction of M-line protein with light meromyosin.
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PMID:Physicochemical studies on the creatine kinase M-line protein and its interaction with myosin and myosin fragments. 79 21


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