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PubMed2003

Potentiometric response mechanism of a poly(acrylamide)-phthalocyaninato tin(II) film coated platinum electrode in acetonitrile and N,N-dimethylacetamide.

A new sensor constructed by a platinum electrode coated with a non-plasticized poly(acrylamide) polymer (PAA) film coupled with phthalocyaninato tin(II) ([Sn(II)(pc)]) was developed. The potentiometric response behavior of this PAA-[Sn(II)(pc)] electrode for such anions as CN-, F-, Cl-, and Br- in dimethylacetamide and acetonitrile were investigated. The electrode showed a Nernstian response to CN- and F- and a quite poor response to Cl- and Br-. The mechanism of the peculiar selective response was studied by cyclic voltammetric and spectrophotometric methods. The voltammetric investigation suggested that the charge of the host compound in the sensor membrane had no effect on the potential response of the electrode. It was also found by a spectrophotometric investigation that the complexing of [Sn(II)(pc)] with CN- and F- lead to the selective response of the electrode. The motive force of the complexing was considered to be a ligand exchange of CN- or F- with molecules at the axial site of [Sn(II)(pc)] due to solvent effects to the interest anions.

Journal Article↗
PubMed1975

[Coupled use of chromatography and acrylamide-agarose gel electrophoresis in the study of polymeric forms of paraproteins].

A study of the physical properties of paraprotein required until now, the use of fairly complicated techniques, such as analytical ultracentrifugation. The use of chromatography on acrylamide agar pearls and electrophoresis on indubiose plates, coupled with the classical techniques of electrophoresis and immunoelectrophoresis, permitted a more simple approach to these problems. The study of IgA paraproteins in several polymerised forms, is an example of the possibilities of this new method of investigation.

Chromatography↗
PubMed1990

A two-dimensional acrylamide gel electrophoresis/computer software approach to decoding the human genome.

The human genome sequencing initiative is sure to be an expensive and time-consuming project. To maximize the quality of the initial thrust, it is necessary to concentrate on sequencing those genes that are actively involved in crucial biological processes, both normal and otherwise. To identify the protein products of these genes, we propose the use of two-dimensional acrylamide gel electrophoresis and powerful computer software. The two-dimensional gels can then be scaled to yield sufficient amounts of the protein for direct amino acid sequence analysis. The amino acid sequence then provides the direct link back to the gene.

Amino Acid Sequence↗
PubMed1975

Observations on trace proteins in plasma of febrile patients by cationic disc electrophoresis in acrylamide gel at pH 3.8.

Cationic disc electrophoresis at pH 3.5 in 6 M urea-containing acrylamide gels permits analysis of plasma and other body fluids for the presence of trace proteins with pI greater than or equal 5 and M.W. less than 60,000. These charge and size characteristics would include rabbit and human granulocytic pyrogen, human monocytic pyrogen and, by inference, other similar candidate pyrogenic proteins. Semiquantitation of the trace protein content can be achieved by densitometric scanning of gels stained with Amido schwarz. Duplicate analyses were performed on plasma samples from 133 individuals: normal, 15; afebrile advanced cancer, 18; afebrile Hodgkin's disease, 30; febrile Hodgkin's disease, 33; other febrile lymphoma, 13; febrile advanced cancer without infection, 12; and pyogenic fever, 12. Plasma from most of the febrile patients, particularly from febrile Hodgkin's disease patients, contained trace proteins not detectable in the afebrile individuals studied. In patients with Hodgkin's disease the quantity of trace proteins present in plasma correlated well with overall severity of Hodgkin's pyrexia, but not with spontaneous hr to hr fluctuations in the fever. Marked reduction in plasma levels of the trace proteins occurred with response to antitumor therapy. Elevated plasma levels of these proteins can be induced by intratumoral inoculation of Bacillus Calmette-Guérin. They appear concomitant with the febrile response.

BCG Vaccine↗
PubMed1977

[Differentiation of Brucella by acrylamide-gel electrophoresis (author's transl)].

The strains of Brucella (Tab. 1) were grown on Tryptose-blood-agar at 37 degrees C, and the strains of Bordetella, Pasteurella and Actinobacillus on blood-agar. After 24 or 48 h they were harvested and extracted in phenol-acetic acid-water solution (4:2:1) (1 ml/50 mg bacterial wet weight) at 4 degrees C over 48 h. After centrifugation (8000 X g, 1 h) 2 volumes of the supernatant were mixed with 1 volume of a 40% sucrose solution in 35% acetic acid. Different volumes (0.20, 0.15 or 0.10 ml) of this were added to 7.5% acrylamide gel (2 ml in tubes 6 X 100 mm), containing 5 M urea and 12% acetic acid. The solution in both electrode chambers was 10% acetic acid. During the first 15 min it was focused with 2 mA/tube, then it was separated for 3 or 5 h with 4 mA/tube. The protein bands were stained with amido black 10B. All species could be exactly differentiated from each other, but the protein bands of biotypes of Bruc. suis, Bruc. melitensis and Bruc. abortus were identical in each case. All investigated strains of Bruc. canis were identical too. A small relationship was noticed between Bruc. canis and Bruc. suis and between Bordetella bronchiseptica and Bruc. canis respectively Bruc. suis strains.

Bacterial Proteins↗
PubMed1967

Peripheral neuropathy with sympathetic overactivity from industrial contact with acrylamide.

This paper describes the experimental and clinical findings of acrylamide intoxication in a human being. It is believed that this is the first such case to be recorded in the medical literature.Acrylamide is widely used as a "chemical grout". It is pumped into dirt, clay and stone walls of excavations in a liquid state together with a catalyst, and it then polymerizes to make a watertight shield.This chemical is neurotoxic in its non-polymerized form and can be absorbed through the intact skin, mucous membranes and lungs. In spite of warnings with regard to its handling, this worker became careless, and developed a contact dermatitis and a polyneuropathy with bluish cold extremities which dripped perspiration.In six months' time after his removal from contact with the chemical the patient made a complete clinical recovery. He was advised not to work with the chemical.

Acrylic Resins↗
PubMed1975

[The differenziation of swine-mycoplasma by acrylamide-gel-electrophoresis (author's transl)].

The strains of swine mycoplasma (Tab. 1) were grown aerobically in Whittlestone's Medium containing swine serum for 4-5 days at 37 degrees C. After centrifugation and washing they were freeze-dried and extracted with a phenol-acetic acid-water solution (4:2:1) (1 ml/5 mg mycoplasma dru weight) at 4 degrees C over 48 h. After centrifugation 2 volumes of the supernatant were mixed with 1 volume of a 40% sucrose solution in 35% acetic acid. 0,15 or 0,2 ml of which were added to the acrylamide-gel (2 ml in a tube 0,5 times 10 cm) containing 5 M urea and 35% acetic acid. This solution was overlayed with 0,1 ml 75% acetic acid and tubes then filled with 10% acetic acid. The solution in both electrode chambers was 10% acetic acid, too. During the first 5 min it was separated with 2 mA/tube, then 3 or 5 h with 4 mA/tube. The protein bands were stained with amido black 10B. For control steril culture medium was investigated, too. Various preparations of freeze-dried M. hyopneumoniae gave identical protein patterns. Nearly identical were the patterns of protein bands from M. suipneumoniae and M. hyopneumoniae; that means identity of the strains or very close relationship (Figs. 1 and 2). This is in agreement with other authors who investigated both strains with serological methods. M. suipneumoniae and M. hyopneumoniae were found to be different as well from M. hyorhinis and M. sp. E9 from M. granularum (Figs. 1 and 2). Between M. hyorhinis and M. sp. E9 less relationship was noted. All these results were in agreement with investigations performed with the aid of Latex agglutination.

Aerobiosis↗
PubMed1977

Chronic toxicity of 2-(2-furyl)-3-(5-nitro-2-furyl) acrylamide (AF-2) in mice, with special reference to carcinogenicity in the forestomach.

Chronic toxicity of 2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide (AF-2), which had been widely used in Japan as a food additive, was studied in both sexes of ICR/JCL mice by feeding a diet containing AF-2 in a concentration of 0.4% or 0.08%. The experiments confirmed its definite carcinogenicity in the forestomach, with dose dependency; more than 70% of mice fed the higher dose developed tumors, the majority of which were squamous cell carcinomas with metastatic growths, whereas, with a lower dose, fewer tumors occurred, following a longer latent period. In addition, possible leukemogenicity was suggested by a higher incidence in AF-2-fed females (10.8%) over that in control females (3.2%). The development of non-neoplastic lesions in the liver and kidneys, and of amyloidosis in various organs was also observed in some of AF-2-fed mice.

Animals↗
PubMed1977

Carcinogenicity of 2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide (AF-2) fed to female Sprague-Dawley rats.

The carcinogenicity of 2-(2-furyl)-3-(5-nitro-5-furyl)acrylamide (AF-2) was investigated by administering it orally to Sprague-Dawley female weanling rats in a grain diet at a dose of 0.2% for 46 weeks, followed by 20 weeks of unmedicated control diet. The total mean cumulative dose of AF-2 was 10.1 g (41.6 mmol) per rat during the 46 weeks of the experiment. Weight gains of rats fed AF-2 was comparable to that of unmedicated control rats. Survival of rats fed AF-2 was 52 +/- 12 (SD) weeds compared to 65 +/- 5 weeks for the unmedicated controls (P less than 0.001). Twenty-four of 29 rats fed AF-2 developed multiple breast tumors, 15 of which were adenocarcinomas. Two of 29 unmedicated control rats had single fibroadenomas of the breast.

Adenocarcinoma↗
PubMed1978

Tartrate-resistant (band 5) acid phosphatase activity measured by electrophoresis on acrylamide gel.

A tartrate-resistant acid phosphatase was isolated from a huma spleen infiltrated with reticulum cells of leukemic reticuloendotheliosis. The purified enzyme was used to establish the optimal conditions for quantitative analysis of this enzyme by electrophoresis on acrylamide gel. As little as 0.1 unit of enzyme activity (or 1 ng of the purified enzyme protein) could be quantitatively detected when it was mixed with 4 mg of albumin before electrophoresis.

Acid Phosphatase↗
PubMed1982

Retention of carcinoembryonic antigen on Sephadex G-50 and acrylamide gel buffer-exchange columns.

We compared the degree of retention of carcinoembryonic antigen on two types of buffer-exchange columns, Sephadex G-50 and acrylamide gel. Both types retained trace amounts of the antigen applied in the form of a perchloric acid extract, as measured by its release into plasma samples subsequently processed through the same columns, Cross contamination, resulting in values falsely high by greater than 1 microgram/L, was observed when columns were re-used after processing plasma samples with carcinoembryonic antigen concentrations greater than 700 micrograms/L.

Blood Chemical Analysis↗
PubMedDate not supplied

[Method of long-term electrophoresis in gradient polyacrylamide gel with a linear change of acrylamide concentration].

The method of long-time protein electrophoresis in a gradient polyacrylamide gel with a linear change of acrylamide concentration along the gel column was used to determine the molecular mass of protein molecules and their geometric sizes. In our investigation great attention was paid to the determination of the molecular form by the peak width in densitograms of protein fractions. Besides experimental data a possible physical interpretation of the essense of empiric equation is suggested.

Electrophoresis, Polyacrylamide Gel↗
PubMedDate not supplied

Analysis of human serum proteins by molecular weight dependent acrylamide gel electrophoresis.

The technique of acrylamide gel electrophoresis of sodium dodecyl sulfate treated protein mixtures has been applied to the analysis of human serum proteins in the 70,000 to 250,000 molecular weight range. After staining, the bands are well defined, the molecular weight is defined and, hence, the identity of each can be estimated from the migration distance. In ambiguous cases, the identification of a band is confirmed by an independent method. The procedure is particularly valuable in the study of the gammopathies. The immunoglobulins migrate as expected, in contrast to the problems often encountered in the Ornstein-Davis gel method. Furthermore, light chains migrate more rapidly, are well separated from other serum proteins and, therefore, are readily detected. Paraproteins from three patients with documented gammopathies have been studied and characterized using this method.

Animals↗
PubMed1977

[Fractionation of chromatin in acrylamide gel with immobilized non-histone proteins and DNA].

Liver and kidney chromatin and DNA were fractionated in acrylamide columns with immobilized readily extracted non-histone chromosomal proteins (RE-NHCP). Chromatin was fractionated in two fractions on the column with RE-NHCP, one of the fractions is sorbing and has a poor protein contents, as compared to the initial chromatin preparation. Fractionation of chromatin in two fractions (sorbing and non-sorbing) was also observed under its chromatography in the column with immobilized DNA. Both chromatin fractions are stripped in the protein content after the elution, which is probably due to the transfer of some proteins from chromatin to immobilized DNA. Chromatography of DNA on gel with homologous RE-NHCP also results in DNA fractionation into sorbing and non-sorbing fractions. The data obtained suggest the irregularity of the distribution and the restriction of "binding sites" for exogenous homologous and heterologous RE-NHCP and of the number of chromatin proteins, which are capable of additional binding with exogenous homologous DNA.

Animals↗
PubMed1998

Large DNA fragment sizing using native acrylamide gels on an automated DNA sequencer and GENESCAN software.

We have investigated the potential of the PE Applied Biosystems Model 373 Automated DNA Sequencer and GENESCAN software to size minisatellite alleles ranging in size from 230 bp to 2.5 kbp. We report on the use of a native (non-denaturing) acrylamide gel system and fluorescent dUTP labeling of PCR products. The observed variability in size calling ranged from +/- 0.4-bp standard deviation (SD) at the lower end of the size range to +/- 37.5-bp SD for the largest allele. Both within-gel and between-gel variability in sizing increased with larger alleles, in particular when sizes exceeded 2 kbp. Size-calling differences were observed dependent on the method used to fluorescently label the PCR products and with the fluorescent dye type and concentration used in incorporation. The benefits and limitations of the current GENESCAN software in sizing large DNA fragments are also discussed.

Alleles↗