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Query: UMLS:C0027960 (mole)
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Four major glycoproteins were extracted by dilute salt solution from procine mitral valvular tissue. Two of these major glycoproteins, procine valve glycoprotein I and porcine valve glycoprotein III, were isolated and purified by fractionation of salt extract with ammonium sulfate followed by column chromatography on DEAE-cellulose. The purified glycoproteins appeared to be homogeneous by polyacrylamide disc electrophoresis in several buffer systems, and by Sephadex filtration. The porcine valve glycoprotein I has a molecular weight of approximately 120000. Isoelectric focusing yielded a single band, pI = 5.8. The glycoprotein contained large amounts of acidic amino acids, and amide nitrogen. The carbohydrate moiety was composed of fucose, mannose, galactose, glucose, glucosamine, and galactosamine in the molar ratio of 5:10:15:12:7:2 per mole of glycoprotein. The second major glycoprotein, porcine valve glycoprotein III, has an approximate molecular weight of 72000. This glycoprotein gives two bands upon analytical isoelectric focusing with isoelectric points of pI = 4.1 and 4.3. Porcine valve glycoprotein III contained large amounts of acidic amino acids and low amounts of amide nitrogen. Its carbohydrate moiety was composed of glucose, galactose, mannose, fucose, glucosamine, and sialic acid in the ratio of 3:3:2:1:4:1 mol/mole of glycoprotein. This glycoprotein was similar to a glycoprotein preparation isolated from porcine aortic intima by P.V. Wagh and B.I. Roberts (1972), Biochemistry 11, 4222.
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PMID:Purification and chemical characterization of salt-extractable glycoproteins from porcine mitral valve. 93 28

Sodium dodecyl sulfate (SDS) binds to pancreatic lipase in a cooperative manner up to about 200 moles/mole of protein. This binding in a rapid and irreversible inactivation of lipase. Bile salts under certain conditions prevent SDS inactivation of lipase when both detergents are present together. Under these conditions bile salts also prevent the binding of SDS to lipase. This effect is parallel to and probably mediated by a decrease in the SDS monomer concentration as the result of the formation of mixed bile salt-SDS micelles.
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PMID:Interactions of pancreatic lipase with bile salts and dodecyl sulfate. 96 41

1. During dehydrocholate administration in the taurine replete dog, the maximum excretory rate of total bile salt (almost entirely dehydrocholate derivative, mostly conjugated) was 3-84 +/- 0-53 (S.D.) mumole/min. kg body wt. (eleven experiments). This was much less than the excretory maximum previously obtained for taurocholate (8-64 +/- 1-31 (S.D.) mumole/min. kg total cholate, mostly conjugated). 2. The superimposition of taurocholate infusion did not cause any significant change in the 'dehydrocholate' maximum but taurocholate itself was excreted into bile at no more than about half its normal maximum. When taurocholate maximum excretion was established first, it was reduced by dehydrocholate administration. In both types of experiment the joint bile salt excretory maximum was of the same order as that of taurocholate alone, provided taurocholate made up at least 40-50% of the total bile salt. 3. When taurocholate administration was stopped, the maximum excretory rate of 'dehydrocholate' rose to values up to 63% above the initially determined excretory maximum; the enhanced 'dehydrocholate' excretory maximum, when calculated for optimal conditions, approached that of actively conjugated vholate, even though the effective 'dehydrocholate' concentration in bile was ten to twenty times the critical micellar concentration of taurocholate. This suggests that the effective bile salt concentration in bile is not an important determinant of the secretory performance of a bile salt. 4. To explain findings (2) and (3) it is necessary to postulate that taurocholate has both a facilitatory and an inhibitory action on 'dehydrocholate' excretion. The facilitatory action, which persists after taurocholate has left the animal, may consist either of an increase in the maximum rate at which modification of dehydrocholate takes place within the liver cell, or an increase in the number of functioning 'carriers' for 'dehydrocholate' transfer. The data suggest that the inhibitory effect is due to the competitive interaction that also appears to exist between the two bile salts. 5. The increase in bile flow rate per unit increase in 'dehydrocholate' excretion (15 ml./m-mole) was about twice that obtained for taurocholate. There was no significant formation of micellar aggregates during 'dehydrocholate' excretion, as judged from the total electrolyte concentration of bile and its osmalality. 6. During the excretion of 'dehydrocholate'-taurocholate mixtures (approximately 1:1) at submaximal rates the associated bile flow rate was not less than the sum of the separate components, thus suggesting that 'dehydrocholate' was not being incorporated in taurocholate mixed micelles.
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PMID:The secretory characteristics of dehydrocholate in the dog: comparison with the natural bile salts. 97 76

Amyloglucosidase from Aspergillus niger (alpha-1,4 and 1,6 glucan glucohydrolase, EC 3.2.1.3) was immobilized through adsorption onto a hexyl-Sepharose, containing 0.51 mol hexyl-group per mole of galactose. The adsporption limit of the carrier with respect to this enzyme was about 17 mg per gram wet conjugate. The retention of activity upon immobilization was high, varying from essentially full activity at low enzyme content down to 68% at the adsorption limit. The immobilized preparation, as well as the soluble enzyme, showed apparent zero order kinetics within 60% of the substrate's conversion limit. Product inhibition of the soluble enzyme showed a KI of 5-10(-2)M. In the presence of 3M NaCl, adsorbates were formed more rapidly and with a higher yield of immobilized protein, but with lower specific activity. Conjugates resulting from adsorption of amyloglucosidase in identical concentrations, but at different salt contents, showed comparable activities and operational stabilities. Continuous operation from three months reduced conjugate activity to 40%. The thermal stability of the adsorbate was inferior to that of the soluble enzyme, but was noticeably enhanced in the presence of substrate.
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PMID:Immobilization of enzymes based on hydrophobic interaction. II. Preparation and properties of an amyloglucosidase adsorbate. 99 Apr 28

Enthalpy of reaction of guanidinium chloride with sodium DNA salt was determined microcalorimetrically at 25 degrees C in water-ethanol solutions of various concentrations. At low ethanol contents (up to 25 mole%) reaction is exothermic, its enthalpy being only slightly dependent on ethanol concentration. Above 28 41 mole % of ethanol reaction becomes endothermic. As above 41 mole% of ethanol in the absence of guanidinium ions A-type DNA conformation appears in the solution, which under the influence of guanidinium is converted to the B-type conformation, enthalpy of conformation transition must be included in the measured enthalpy of the reaction. Dependence of the measured enthalpy on ethanol concentration in the B--A transition region testifies to a very small value of the enthalpy change during this transition.
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PMID:[Estimation of the enthalpy of B--A transitions in DNA in water-ethanol solutions]. 100 64

As glycerol was suggested as an osmotic agent in the salt tolerant Debaryomyces hansenii the concentrations of total, intracellular, and extracellular glycerol produced by this yeast was followed during growth in 4 mM, 0.68 M, and 2.7 M NaCl media. The total amount of glycerol was not directly proportional to biomass production but to the cultural salinity with maximum concentrations just prior to or at the beginning of the stationary phase. In all cultures the cells lost some glycerol to the media, at 2.7 M NaCl the extracellular glycerol even amounted maximally to 80% of the total. A distinct maximum of intracellular glycerol, related to dry weight or cell number, appeared during the log phase at all NaCl concentrations. As the intracellular calculated glycerol concentrations amounted to 0.2 M, 0.8 M, and 2.6 M in late log phase cells at 4mM, 0.68 M, and 2.7 M NaCl, respectively, whereas the corresponding analysed values for the glycerol concentrations of the media were 0.7 mM, 2.5 mM, and 3.0 mM, glycerol contributes to the osmotic balance of the cells. During the course of growth all cultures showed a decreasing heat production related to cell substance produced, most pronounced at 2.7 M NaCl. At 2.7 M NaCl the total heat production amounted to--1690 kJ per mole glucose consumed in contrast to--1200 and--1130 kJ at 4 mM and 0.68 M NaCl, respectively. The Ym-values were of an inverse order, being 129, 120, and 93 at 4 mM, 0.68 M, and 2.7 M NaCl respectively.
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PMID:On the mechanism of salt tolerance. Production of glycerol and heat during growth of Debaryomyces hansenii. 101 45

Kinetic results of the crystal growth and dissolution of seed crystals of calcium fluoride and magnesium fluoride, obtained conductimetrically and potentiometrically, indicate that both processes are controlled by a surface reaction mechanism. An initial reaction surge in the case of magnesium fluoride is consistent with a concomitant secondary nucleation process. The activation energies for the growth and dissolution of calcium fluoride, 14.5 and 1.4 kcal mole-1, also point to surface reaction control. The heat of solution of this salt, obtained calorimetrically, was 2.9 +/- 0.1 kcal mole-1.
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PMID:Kinetics of crystal growth and dissolution of calcium and magnesium fluorides. 106 44

The reactions of hydrated electrons produced during pulse radiolysis have been utilized to investigate the binding of ethidium bromide to heparin. Complexes of ethidium bromide and heparin can be dissociated with salt. Divalent cations are more effective than monovalent cations in this respect. Pulse-radiolysis investigations at different temperatures indicate that the thermodynamic parameters governing the interaction of ethidium bromide with heparin are deltaH' = 11-6 kcal mole-1 and deltaS' = 42-6 cal deg-1 mole-1.
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PMID:Interaction of ethidium bromide with heparin. 108 22

The binding of conjugated bile salts to pancreatic colipase and lipase has been studied by equilibrium dialysis and gel filtration. The results indicate that at physiological ionic strength and pH, conjugated bile salts bind as micelles to colipase: 12-15 moles/mole of colipase for the dihydroxy conjugates and 2-4 for the trihydroxy conjugates. No binding of bile salt takes place from monomeric solutions. Under the same experimental conditions, only 1-2 moles of conjugated dihydroxy bile salts bind to pancreatic lipase.
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PMID:Binding of bile salts to pancreatic colipase and lipase. 117 Feb 69

The thermal denaturations of type I human placenta collagen were studied in different aqueous solutions in the temperature range from 274 to 345 K by differential scanning calorimetry. The thermodynamic parameters of denaturational process were accurately. The average temperature of denaturation of the collagen Td is 47.1 degrees C, and the denaturational enthalpy delta Hd is 8.43 kJ per mole of residue in salt-free aqueous solution at pH 3.7. The linear relationship of delta Hd with Td has been obtained for the various collagens studied. The various factors concerning the stabilization of collagen structure of the Sigma collagen have been demonstrated. The dominant factors are hydrogen bonding and the participation of water molecules in the collagen structure. It is concluded from the thermodynamic evidence obtained that the water-carbonyl model is preferable to other models. By means of calculating the van't Hoff enthalpy of the collagen denaturation, the number and the size of cooperative blocks of the Sigma collagen have been evaluated. Its molecule contains five cooperative blocks, each having 600 residues or so. The type I human placenta collagen is a multi-domain protein.
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PMID:Calorimetric study of thermal denaturation of type I human placenta collagen. 128 46


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