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

The chemical composition of axoplasm extracted from the giant axon of Myxicola infundibulum has been analysed, and some of the factors which disperse its gel structure have been identified. 2. The axoplasm contains about 3-6% protein, and 0-12% lipid. It is isosmotic with sea water and has a pH near 7-0. 3. Inorganic ions in extracted axoplasm include: Na+, 13m-mole/kg wet wtl; K+, 280; Cl-, 24; Ca2+, 0-3; Mg2+, 3. 4. Free organic ions in axoplasm include: gly, 180 m-mole/kg wet st.; cysteic acid, 120; asp, 75; glu, 10; ala, 7; tau, 5; thr, 2; gln and ser, trace; homarine, 63; isethionate, 0. 5. The gel structure is dispersed by solutions containing 1--10 mM-Ca2+, because this ion activates an endogenous protease. The gel can also be dispersed without proteilysis by solutions containing 0-5 M-KCl, or 0-5 M guanidine hydrochloride, or 3-5 M urea, all of which break down neurofilaments. 6. It is argued that many aspects of the composition and dispersal properties of Myxicola axoplasm are similar to those in other axons.
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PMID:Axoplasm chemical composition in Myxicola and solubility properties of its structural proteins. 0 Dec 60

An automated AutoAnalyzer method using 5:5'-dithiobis-2-nitrobenzoic acid is described for determining whole blood glutathione reductase (BGR) activity and for measuring in vitro activation of BGR with flavin adenine dinucleotide (FAD). BGR activity is expressed as mumoles glutathione regenerated from oxidized glutathione per ml of whole blood (WB) or per g of hemoglobin. The stimulatory effect of FAD on BGR activity divided by the activity without FAD determined the activity coefficient (AC). We found that NADPH and oxidized glutathione assay concentrations of 0.100 mmole/liter and 0.250 mmole/liter, respectively, in 0.1 mole/liter phosphate buffer, pH 7.4, gave consistent results when WB, before assay, was diluted 20-fold. WB samples to be stored are initially diluted 10-fold with distilled water and frozen. Prior to assay, two aliquots of the sample are diluted 2-fold, one aliquot with distilled water and another with 46 mumole/liter FAD. With sample and manifold dilutions the assay FAD concentrations is 1.0 mumole/liter: assay concentrations greater than 5.0 mumole FAD/liter were shown to be inhibitory. We examined blood samples from 617 children in the age range 6 to 60 months and determined the normal AC range to be between 1.00 and 1.35. Six weaned rats (23 days of age), maintained on a riboflavin-deficient diet, showed a mean AC of 1.23, 1.54, 2.02, and 2.41 at 23, 26, 30, and 36 days of age, respectively. Six control rats maintained an AC of 1.23 +/- 0.05 (SD) during the same period.
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PMID:An automated flavin adenine dinucleotide-dependent glutathione reductase assay for assessing riboflavin nutriture. 0 81

The effects of electrolytes on the self-association of the antihistaminic drugs, tripelennamine hydrochloride, thenyldiamine hydrochloride, pyrilamine maleate, pheniramine maleate, chlorpheniramine maleate, and brompheniramine maleate, in aqueous solution were examined by light-scattering from tripelennamine bydrochloride and thenyldiamine hydrochloride in 0.154 mole of sodium chloride/kg and 0.150 mole of sodium maleate/kg indicated a micellar pattern of aggregation. Higher aggregation numbers and lower CMC's were determined in the presence of the maleate ion. No significant discontinuity in the concentration dependence of the light scattering of the remaining compounds in either of the two electrolytes was evident, and the aggregation of these compounds was treated using a stepwise association model. Values of the association constants and the limiting number of associating species were, in general, increased by the addition of electrolyte in the order water less than sodium chloride less than sodium maleate. An apparently nonmicellar pattern of aggregation could be induced by chemically changing the counterion from chloride to maleate.
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PMID:Aggregation of antihistamines in aqueous solution: effect of counterions on self-association of pyridine derivatives. 0 28

The amide content of neocarzinostatin (NCS), an antitumor protein, has been determined by analysing asparagine and glutamine in the Pronase-aminopeptidase M digests of tetra-S-carboxymethyl-NCS and carboxyl-modified NCS (modified with a water-soluble carbodiimide and [14C]glycine methyl ester). Preneocarzinostatin (PRE) was separated and purified from a crude NCS preparation by CM-cellulose column chromatography. PRE was found to contain one mole less asparagine than NCS, and asparagine was deamidated to aspartic acid in PRE. A time-dependent conversion of NCS to PRE at pH 3.2 at 4 degrees or in 0.1 M acetic acid at 26 degrees was studied in two ways; first, by quantitative determination of NCS and PRE by CM-cellulose column chromatography and second, by following the release of free NH3 during dialysis in an air-tight container. Within experimental error, PRE was indistinguishable from NCS in amino acid content after acid hydrolysis, as well as in apparent molecular weight as determined by SDS-disc gel electrophoresis (10% acrylamide), and N- and C-terminal amino acid residues. Both NCS and PRE shared a common antigenicity as determined by Ouchterlony's agar diffusion method. Only a slight difference between the two in electrophoresis on a cellulose acetate membrane and on a peptide map of the tryptic digest was demonstrated. PRE, however, was completely devoid of biological activity. In addition to the chromatographic difference, a conformational difference was observed by CD spectroscopy, namely, an apparently looser structure of PRE was indicated by the shallowness of the trough in the 240-265 nm region. This interpretation was supported by the finding that digestions by Pronase were more extensive with PRE than with NCS. These results indicate an important role of the single asparagine residue (Asn 83) of NCS in the biological activity, which is evidently governed by the conformation.
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PMID:Spontaneous deamidation of a protein antibiotic, neocarzinostatin, at weakly acidic pH. Conversion to a homologous inactive preneocarzinostatin due to change of asparagine 83 to aspartic acid 83 accompanied by conformational and biological alterations. 1 34

12 prealbumines of rat brain water-soluble fraction were studied. Neither lipid components nor carbohydrate ones were found out in the proteins. Three of the proteins appeared to be RNA-proteids. Their subcellular distribution was investigated. The effects of temperature, salts, acids and ethanol on disc electrophoretic spectrum of brain prealbumines were closely observed. The amino acid composition, properties, compartmentation, tissue and species specificity of one of the prealbumines were studied in detail. The protein is marked as BTB-protein, as it migrates under disc electrophoresis in 7,5% polyacrylamide gel with the "witness" front of bromothemol blue (BTB). The content of BTB-protein is 0.06--0.08 gr per 100 gr of wet tissue. The protein is RNA-proteid. Its molecular weight is 10,000--20,000. BTB-protein contains 42 mole % of acidic amino acids and 5.4 mole % of alkaline ones. The protein was found in nuclear and cytoplasmic fractions. It is mainly an all-organs protein. Small amount of this protein is found in blood serum. BTB-protein can be found on the disc electrophoregramms of embryo and newborn rats brain proteins, as well as of the brain of other mammals, birds and amphibia. BTB-protein is resistant to boiling and to the effects of salts, acids, ethanol. It is suggested that BTB-protein has heterogenous structure and may be of neurophysin nature.
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PMID:[Investigation of rat brain prealbumins]. 1 53

The method of solution and puridication of hydrogenase from chromatophores of purpur sulphur bacteria Thiocapsa roseopersicina strain BBS are described. Hydrogenase molecular weight is 73000. It contains 4,4 mole S2- and 3.1 mole Fe2+ per mole of protein; pI 4.15. The enzyme absorption spectrum has the maximun et 400-410 nm, which is characteristic of proteins containing non-haem iron. Membrane--linked enzyme as well as soluble hydrogenase of that microorganism is characterized by high thermal stability: inactivation occurs at the temperature above 78 degrees C when the optimal temperature for that enzyme is 70 degrees C. Homogenous enzyme catalyses D2--H2O exchange reaction, reversible redox reaction of methyl viologene and benzyl viologene.
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PMID:[Purification and properties of phototrophic bacteria Thiocapsa roseopersicina hydrogenase bound with chromatophores]. 1 62

1. The total Mg in isolated fibres of Balanus aquila was 10-5 m-mole/kg wet wt. 2. The intracellular free Mg was measured by a null point method using Eriochrome Blue as an indicator of free Mg, and internal dialysis with solutions of varying ionized Mg concentrations. The results indicated a free Mg of 6 mM or 4-2 m-mole/kg wet wt. in the intracellular water immediately surrounding the dialysis capillary. 3. The ATP concentration was estimated to be 4-9 m-mole/kg wet wt. 4. A tentative partitioning of Mg among various intracellular constitutents based on present data combined with published work by others is (m-mole/kg wet wt): free, 4-2; MgATP, 4-2; myofibrillar bound, 1; residual (presumably bound to arginine phosphate and phosphate) ca. 1.
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PMID:The concentration of ionized magnesium in barnacle muscle fibres. 1 2

1. Urea and water permeabilities of chicken erythrocytes are considerably lower than those of mammalian red cells. 2. The permeabilities to urea, thiourea and to N-methylurea (about 10(-6) cm/sec at 25 degrees C) were independent of concentration within a very broad range, and we found no evidence of interaction between transport of analogue molecules. The activation energies were between 17 and 19 kcal/mole, and urea transport was not inhibited by phloretin, which inhibits urea transport in mammalian red cells. 3. The water permeability of chicken red cells (as measured by the diffusion of tritiated water) was 1-35 X 10(-3) cm/sec at 25 degrees C. The activation energy was 10 kcal/mole, and the water permeability was not affected by phloretin or parachloromercuribenzoate. 4. It is concluded that the urea and water permeabilities of the chicken erythrocyte membrane are similar to those of a non-porous bimolecular phospholipid membrane. 5. Like the red cells of other animal species the chicken red cell membrane contains an anion transport system, mediating a rapid exchange of chloride across the cell membranes. The pH dependence, temperature dependence, and sensitivity to inhibitors were similar to the properties of the anion transport system found in mammalian red cells. Our study shows, therefore, that the transport system offers a highly specific pathway to the exchange of anions, without presenting an inspecific leak to the permeation of water and urea.
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PMID:Separative pathways for urea and water, and for chloride in chicken erythrocytes. 1 3

Methods were developed for quantitating epimerization to epihetacillin and hydrolysis to ampicillin in the alkaline degradation of hetacillin, and both rates in deuterium oxide at 35 degrees and in water at various temperatures were determined. In each case, plots of log k for the epimerization against pH or pD yielded straight lines with a positive slope, which verified the first-order dependence on the hydroxide ion or deuteroxide ion. The activation energy of the epimerization process was 21.2 kcal/mole. In aqueous solution at high pH, epimerization rather than conversion to ampicillin represents a major pathway of hetacillin degradation, although the beta-lactam ring of the hetacillin molecule is highly resistant to attack by the hydroxide ion.
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PMID:Hydrolysis and epimerization kinetics of hetacillin in aqueous solution. 1 91

The aminoglycoside antibiotics fortimicins A and B produced by a naturally occurring strain Micromonospora sp. MK-70 were isolated from its fermentation beer. Fortimicins A and B were isolated as water-soluble, basic, white amorphous powders having molecular formula C17H35N5O6 and C15H32N4O5, respectively. Acid hydrolysis of fortimicin A indicated that it has one mole of glycine in its molecule while fortimicin B has not. Paper chromatography, silica-gel and carbon thin-layer chromatography revealed that fortimicins A and B are novel aminoglycoside antibiotics.
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PMID:Fortimicins A and B, new aminoglycoside antibiotics. II. Isolation, physico-chemical and chromatographic properties. 1 8


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