CONDUCTANCES OF AQUEOUS SOLUTIONS OF SODIUM HEXANOATE (SODIUM CAPROATE) AND THE LIMITING CONDUCTANCES OF THE HEXANOATE ION, AT 25 °C AND 35 °C

1960 ◽  
Vol 38 (10) ◽  
pp. 1939-1945 ◽  
Author(s):  
A. N. Campbell ◽  
J.I. Friesen
Keyword(s):  
Molecular Weight ◽  
Aqueous Solutions ◽  
Stokes Equation ◽  
Apparent Molecular Weight ◽  
Ionic Micelles ◽  
Limiting Conductances ◽  
Limiting Equivalent Conductances

The equivalent conductances, densities, and viscosities of aqueous solutions of sodium hexanoate have been determined at 25 °C and 35 °C at concentrations ranging from 0.0003 M to saturation.The limiting equivalent conductances of the hexanoate ion have been determined as 27.37 ± 0.04 mhos at 25 °C and 34.69 ± 0.05 mhos at 35 °C.The Robinson–Stokes and the Falkenhagen–Leist equations have been applied to the data. The Robinson–Stokes equation reproduces the data within 0.7 mho up to 0.5 M at 25 °C when å = 13 Å. At 35 °C the data are reproduced within 0.5 mho up to 0.05 M with å = 10 Å. The Falkenhagen–Leist equation reproduces the data at 25 °C within 0.4 mho up to 0.1 M with å = 5.5 Å. An å = 4.0 Å reproduces the 35 °C data within 0.5 mho up to 0.05 M.From the form of the conductance curves and from an estimation of the apparent molecular weight it was concluded that the hexanoate ion does not form ionic micelles.

THE LIMITING EQUIVALENT CONDUCTANCES OF AMMONIUM CHLORIDE, AMMONIUM BROMIDE, AND AMMONIUM NITRATE AT 35.00 °C.

1958 ◽  
Vol 36 (2) ◽  
pp. 330-338 ◽  
Author(s):  
A. N. Campbell ◽  
E. Bock
Keyword(s):  
Aqueous Solutions ◽  
Ammonium Nitrate ◽  
Ammonium Chloride ◽  
Stokes Equation ◽  
Probable Error ◽  
Ammonium Bromide ◽  
Conductance Data ◽  
Ionic Conductances ◽  
Hydrolysis Of ◽  
Limiting Equivalent Conductances

The limiting equivalent conductances of ammonium chloride, ammonium bromide, and ammonium nitrate as well as the limiting ionic conductances of the ammonium and nitrate ions were determined at 35 °C. with a probable error of 0.05%. The values found were [Formula: see text] 180.97 mhos, [Formula: see text] 182.73 mhos, [Formula: see text] 174.21 mhos, [Formula: see text] 88.73 mhos, and [Formula: see text] 85.48 mhos. These values were obtained by the application of the Shedlovsky method of extrapolation to equivalent conductance data, which had been corrected for the hydrolysis of the ammonium ion.Observed equivalent conductances of aqueous solutions of ammonium nitrate at 35 °C., in the concentration range from 0.0002 N to 10 N, have been compared with those calculated by means of the Wishaw–Stokes and Falkenhagen–Leist equations. The Wishaw–Stokes equation was found to give better agreement with experiment than the Falkenhagen–Leist equation.

Conductances of electrolytes in solutions of the sucrose polymer Ficoll

1964 ◽  
Vol 17 (3) ◽  
pp. 304 ◽  
Author(s):  
RH Stokes ◽  
IA Weeks
Keyword(s):  
Aqueous Solutions ◽  
Polymer Molecules ◽  
Sucrose Solutions ◽  
Limiting Conductances ◽  
Limiting Equivalent Conductances

The limiting equivalent conductances of several electrolytes have been measured at 25� in aqueous solutions of the synthetic sucrose polymer Ficoll. Though the viscosity of the solutions is several times that of sucrose solutions of the same percentage by weight of solute, the limiting conductances of small ions in them are little different from those in sucrose solutions. It is concluded that the polymer molecules form loose networks to a large extent permeable to small ions.

Physico-Chemical Properties of Recombinant Desulphatohirudin

1990 ◽  
Vol 63 (03) ◽  
pp. 499-504 ◽  
Author(s):  
A Electricwala ◽  
L Irons ◽  
R Wait ◽  
R J G Carr ◽  
R J Ling ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Gel Filtration ◽  
Chemical Properties ◽  
Alpha Helix ◽  
Apparent Molecular Weight ◽  
Correlation Spectroscopy ◽  
Nmr Studies ◽  
Recombinant Hirudin ◽  
Physico Chemical ◽  
Recombinant Molecule

SummaryPhysico-chemical properties of recombinant desulphatohirudin expressed in yeast (CIBA GEIGY code No. CGP 39393) were reinvestigated. As previously reported for natural hirudin, the recombinant molecule exhibited abnormal behaviour by gel filtration with an apparent molecular weight greater than that based on the primary structure. However, molecular weight estimation by SDS gel electrophoresis, FAB-mass spectrometry and Photon Correlation Spectroscopy were in agreement with the theoretical molecular weight, with little suggestion of dimer or aggregate formation. Circular dichroism studies of the recombinant molecule show similar spectra at different pH values but are markedly different from that reported by Konno et al. (13) for a natural hirudin-variant. Our CD studies indicate the presence of about 60% beta sheet and the absence of alpha helix in the secondary structure of recombinant hirudin, in agreement with the conformation determined by NMR studies (17)

The Activation of Human Factor IX

1975 ◽  
Vol 33 (03) ◽  
pp. 553-563 ◽  
Author(s):  
B Østerud ◽  
K Laake ◽  
H Prydz
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl ◽  
Apparent Molecular Weight ◽  
Factor Ix ◽  
Factor Vii ◽  
Activate Factor ◽  
Human Factor Ix ◽  
Factor Xia ◽  
Tissue Thromboplastin ◽  
Native Factor

SummaryThe activation of factor IX purified from human plasma has been studied. Factor XIa and kallikrein separately activated factor IX to factor IXa. In both cases factor IX a had an apparent molecular weight of about 42–45000 in sodium dodecyl sul-phate-polyacrylamide disc gel electrophoresis compared with a molecular weight of about 70000 for the native factor IX. The activation by XIa required Ca2+-ions whereas Ca2+-ions did not influence the activation by kallikrein. A mixture of tissue thromboplastin and factor VII or RusselPs-viper venom alone did not activate factor IX. Trypsin activated and plasmin inactivated factor IX.

scholarly journals Nuclear matrix of HeLa S3 cells. Polypeptide composition during adenovirus infection and in phases of the cell cycle.

1977 ◽  
Vol 72 (1) ◽  
pp. 194-208 ◽  
Author(s):  
L D Hodge ◽  
P Mancini ◽  
F M Davis ◽  
P Heywood
Keyword(s):  
Cell Cycle ◽  
Molecular Weight ◽  
Nuclear Matrix ◽  
Apparent Molecular Weight ◽  
Molecular Weight Range ◽  
Weight Range ◽  
Molecular Weights ◽  
Liver Nuclei ◽  
Hela S3 ◽  
Biochemical Analyses

A subnuclear fraction has been isolated from HeLa S3 nuclei after treatment with high salt buffer, deoxyribonuclease, and dithiothreitol. This fraction retains the approximate size and shape of nuclei and resembles the nuclear matrix recently isolated from rat liver nuclei. Ultrastructural and biochemical analyses indicate that this structure consists of nonmembranous elements as well as some membranous elements. Its chemical composition is 87% protein, 12% phospholipid, 1% DNA, and 0.1% RNA by weight. The protein constituents are resolved in SDS-polyacrylamide slab gels into 30-35 distinguishable bands in the apparent molecular weight range of 14,000 - 200,000 with major peptides at 14,000 - 18,000 and 45,000 - 75,000. Analysis of newly synthesized polypeptides by cylindrical gel electrophoresis reveals another cluster in the 90,000-130,000 molecular weight range. Infection with adenovirus results in an altered polypeptide profile. Additional polypeptides with apparent molecular weights of 21,000, 23,000, and 92,000 become major components by 22 h after infection. Concomitantly, some peptides in the 45,000-75,000 mol wt range become less prominent. In synchronized cells the relative staining capacity of the six bands in the 45,000-75,000 mol wt range changes during the cell cycle. Synthesis of at least some matrix polypeptides occures in all phases of the cell cycle, although there is decreased synthesis in late S/G2. In the absence of protein synthesis after cell division, at least some polypeptides in the 45,000-75,000 mol wt range survive nuclear dispersal and subsequent reformation during mitosis. The possible significance of this subnuclear structure with regard to structure-function relationships within the nucleus during virus replication and during the life cycle of the cell is discussed.

Apparent molecular weight of the substance P binding site in rat brain

1988 ◽  
Vol 152 (1-2) ◽  
pp. 171-174 ◽  
Author(s):  
Yoshihiro Nakata ◽  
Chie Hiraoka ◽  
Tomio Segawa
Keyword(s):  
Molecular Weight ◽  
Substance P ◽  
Binding Site ◽  
Rat Brain ◽  
Apparent Molecular Weight

Detection of inducible nitric oxide synthase inSchistosoma japonicumandS. mansoni

2004 ◽  
Vol 78 (1) ◽  
pp. 47-50 ◽  
Author(s):  
X.-C. Long ◽  
M. Bahgat ◽  
K. Chlichlia ◽  
A. Ruppel ◽  
Y.-L. Li
Keyword(s):  
Nitric Oxide ◽  
Molecular Weight ◽  
Inducible Nitric Oxide Synthase ◽  
Mouse Liver ◽  
Apparent Molecular Weight ◽  
Western Blots ◽  
Oxide Synthase ◽  
Host Tissues ◽  
Inducible Nitric Oxide

AbstractSchistosoma japonicumandS. mansoniwere tested for reactivity with an anti-inducible nitric oxide (iNOS) antibody and the distribution of iNOS was studied by immunofluorescent tests in different stages of the parasites. Reactivity was associated with the tegument in both larval schistosomes (sporocysts and cercariae) and eggs. With adult worms, the majority of the immunofluorescence was predominantly subtegumental inS. japonicumand parenchymal inS. mansoni. Fluorescence was also observed in host tissues (snails and mouse liver). In Western blots, the enzyme ofS. japonicumhad an apparent molecular weight of about 210 kDa. The possible role of worm and host iNOS in the parasite–host interrelation remains to be clarified.

Partial characterization of cheese-ripening proteinases produced by the yeastKluyveromyces lactis

1983 ◽  
Vol 50 (4) ◽  
pp. 469-480 ◽  
Author(s):  
Paul A. Grieve ◽  
Barry J. Kitchen ◽  
John R. Dulley ◽  
John Bartley
Keyword(s):  
Molecular Weight ◽  
Kluyveromyces Lactis ◽  
Apparent Molecular Weight ◽  
Aminopeptidase Activity ◽  
Carboxypeptidase Y ◽  
Casein Hydrolysis ◽  
Cheese Ripening ◽  
Caseinolytic Activity ◽  
Proteinase A

SUMMARYAn extract ofKluyveromyces lactis416 and a β-galactosidase preparation (Maxilact 40000) contaminated with proteinase, showed similar pH profiles of caseinolytic activity. Similar modes of casein hydrolysis (κ-, > αs-, ≥ β-) were observed at pH 5·0 (the pH of Cheddar cheese), without detection of bitterness. The contaminated Maxilact preparation contained similar proteinase types to those detected in an autolysate ofK. lactis. Both the autolysate and the Maxilact preparation contained acid endopeptidase (proteinase A), serine endopeptidase (proteinase B) and serine exopeptidase (carboxypeptidase Y) activities. Some aminopeptidase activity was also detected in both preparations. There were some differences in apparent molecular weight and charge properties between proteinase A and B and carboxypeptidase Y from the 2 proteinase sources.

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