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At least 19 recordsLinked to original sources
PubMed1979

Effect of interaction of aluminum hydroxycarbonate gel and magnesium hydroxide gel on acid neutralization.

Acid neutralization by mixtures of aluminum hydroxycarbonate gel and magnesium hydroxide gel differs from the sum of the acid neutralization of each gel. Acid neutralization by magnesium hydroxide gel in the mixture is not observed until after a substantial portion of the aluminum hydroxycarbonate gel has reacted with acid, even though magnesium hydroxide gel is the faster reacting of the two gels. It is hypothesized that amorphous aluminum hydroxycarbonate forms a coating on the crystalline magnesium hydroxide particles due to electrostatic attraction. This coating prevents protons from reaching the highly reactive magnesium hydroxide until the coating is dissolved by the acid neutralization of aluminum hydroxycarbonate.

Acids↗
PubMedDate not supplied

A comparison of gel-to-gel and skin measurements of electrode impedance.

Utilizing an automated test system, measurements of the 10-Hz impedance were made with electrode pairs joined gel-to-gel and electrode quartets on the skin of the backs of human volunteers. Two skin preparation procedures were examined. As a minimum skin preparation, the electrodes were applied to clean, dry skin from which body hair had been shaved if necessary. As a maximal preparation, the electrodes were applied after mild abrasion of the skin with fine emery cloth. Although the impedances measured for electrodes applied to mildly abraded skin correlated well with measurements made with electrodes of the same brand joined gel-to-gel, virtually no correlation was found if the electrodes were affixed to clean, dry skin.

Adult↗
PubMed1978

Polyacrylamide gel electrophoresis of visna virus polypeptides isolated by agarose gel chromatography.

The proteins of visna are separated into nine major peaks by agarose gel chromatography in 6 M guanidine hydrochloride (GuHCl). The polypeptides in eack peak were isolated by acid precipitation and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The patterns of SDS-PAGE show that the excluded material from the GuHCl column contains an aggregate of 10 non-glycosylated polypeptides. It is shown that this aggregate represents virus substructures that are not completely solubilized by GuHCl. Two glycoproteins, gp175 and gp115, were isolated from the column eluate. The major glycoprotein gp115 was coeluted with P90, P68, and P61 in GuHCl 4. Each of the four major peaks (GuHCl 5 to 8) contains more than one nonglycosylated polypeptide. However, a small polypeptide, P12, can be isolated in a homogeneous form in the last peak, GuHCl 9. Analysis of the virus proteins (100 microgram) by SDS-PAGE shows that 20 radioactive bands can be recognized. During fractionation of the protein on agarose gel columns followed by analysis with SDS-PAGE, a number of minor polypeptides that were not detected before became clearly recognizable. Thus, the combined use of column chromatography and SDS-PAGE shows that visna virus is composed of 25 proteins.

Chromatography, Agarose↗
PubMed1976

The separation of plasma lipoproteins using gel electrofocusing and polyacrylamide gradient gel electrophoresis.

Polyacrylamide gel electrofocusing and gradient electrophoresis have been used to separate the lipoproteins in whole plasma and in fractions prepared by sequential flotation in the ultracentrifuge and by precipitation with dextran sulphate and manganous chloride. After the two-dimensional separation, high density lipoproteins appear as a zone showing noticeable heterogeneity with respect to both isoelectric point and molecular weight. Low density lipoproteins are resolved as a compact spot while very low density lipoproteins are visible as a long horizontal streak across the top of the electrophoresis gel. The implications of the technique for the analysis of lipoprotein patterns in pathological plasmas are discussed.

Electrophoresis, Agar Gel↗
PubMed1975

Micrococcus lysodeikticus ATPase. Purification by preparative gel electrophoresis and subunit structure studied by urea and sodium dodecylsulfate gel electrophoresis.

Micrococcus lysodeikticus ATPase was purified by preparative gel electrophoresis after its "shodk wash" release from the membrane. The method afforded the highest yield of pure protein in the minimum time as compared with former purification procedures. The pure protein had a specific activity of 7 mumol Pi-min- minus 1-mg- minus 1 with incubation times not longer than 3 min, 345 000 mol. wt and was not stimulated by trypsin. By gel electrophoresis at alkaline pH (8.5) in 8 M urea or in sokium dodecylsulfate, the ATPase revealed a complex pattern with two major subunits (alpha and beta) and two minor ones (gamma and delta). The non-identity between the major subunits was demonstrated.

Adenosine Triphosphatases↗
PubMed1979

Gamma globulins of CSF and serum in multiple sclerosis: isoelectric focusing on polyacrylamide gel and agar gel electrophoresis.

Cerebrospinal fluid (CSF) and serum from 139 patients with MS were analyzed with electrophoresis on agar gel (AGE) and isoelectric focusing (IEF) on polyacrylamide gel. In both methods, 82 percent of the patients had abnormal patterns of oligoclonal IgG bands in the gamma globulin and alkaline regions. With IEF, 10 percent of the serum samples contained faint bands corresponding to the bands in CSF. Most of the bands were found in the cathodal part of the alkaline IEF region, but there was no correlation with clinical characteristics. Each patient seems to have a special band pattern which does not change throughout the disease. The gamma-trace protein was seen in 77 percent of the patients on IEF and in 29 percent on AGE. On IEF it appeared at two positions, at pH 8.0 and 9.3, but about 10 other bands were seen in the "normal" alkaline CSF region, making the band pattern of IEF more difficult to interpret than that of AGE. This limits the routine clinical value of IEF, even if the high resolution capacity of this method is useful in research.

Adolescent↗
PubMed1975

Affinity chromatography on hydroxyalkyl methacrylate gels. II. Isolation of thiol-containing protein and peptide using mercurial derivatives of gels.

Absorption properties of hydroxyalkyl methacrylate gels containing various amounts of mercuri derivatives of p-acetaminophenoxyethyl methacrylates (Hg-APEMA) and methacrylanilide (Hg-MAA) were investigated by means of a reduced Ellman's agent (5,5'-dithiobis-2-nitrobenzoic acid) and papain. The optimum gel was used for the affinity chromatography of SH-protease from beans and for the isolation of a peptide with a free sulphhydryl group from the chymotryptic hydrolyzate of serum albumin.

Buffers↗
PubMed1977

A gel filament as an analytical tool: the testing of an affinity chromatographic, product-immobilizing linear gel for determination of enzymatic activity.

A new technique for quantitative analysis is proposed. An underfined volume of the test solution is exposed to a reagent in the form of a gel filament of capillary dimensions. The linear progress in the gel of the compound in question is followed with the aid of the coloured reaction products deposited along its path. With the use of the enzyme gamma-glutamyl transpeptidase it is shown that the velocity in the system of the component to be analysed, as determined by measurement of its coloured track, is related to its activity in the test solution.

Aniline Compounds↗
PubMed1977

Polyacrylamide gel electrophoretic analysis of herpes simplex virus type 1 immunoprecipitates obtained by quantitative immunoelectrophoresis in antibody-containing agarose gel.

Crossed immunoelectrophoresis was used to characterize herpes simplex virus type 1 (HSV-1) antigens produced by infected HEp-2 cells. We report on a method for analyzing the polypeptide content in individual antigen-antibody precipitates eluted from the second-dimensional agarose gel. Four glycoprotein antigens of HSV-1, Ag-8, Ag-11, Ag-6, and Ag-3, were isolated and analyzed for polypeptide content. The molecular weights of the polypeptides are presented.

Antigens, Viral↗
PubMed1977

Humic-like substances of bacterial origin. II. Fractionation of the bacterial humic-like substances by gel filtration on sephadex gels.

Humic-like substances obtained from cells of Pseudomonas acidovorans were separated on Sephadex G-25 into two groups of substances of different molecular weight. The substances of the molecular weight greater than 5000 were successively separated on Sephadex gels G-50, G-75, G-100. Five fractions of different molecular weight were obtained, the percentage of which varied depending on the media used and time of incubation of the bacteria. Most (38%--46%) of the compounds contained in the bacterial humic acids were of approximate molecular weight of 40 000--50 000. The distribution of the fractions in the bacterial "humic-acids" was compared with those of the humic acid made by Fluka A. G. The synthetic humic acid contained most (approximately 40%) of the compounds of approximate molecular weight of 8000--10 000. In the bacterial and synthetic material the content of the compounds with the molecular weight above 100 000 was very similar (8%--12%).

Chromatography, Gel↗