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Degradation of nitrocellulose by fungi.

Three lignocellulolytic fungi, Trametes versicolor, Pleurotus ostreatus, and Coprinus cinereus, and two cellulolytic fungi Trichoderma reesei and Chaetomium elatum were tested for their ability to degrade nitrocellulose. They were provided with different carbon and nitrogen sources in liquid cultures. Nitrocellulose (N content above 12%) was added as nitrogen source (in solution in acetone) alongside amino acids or as sole N source. Either starch or carboxy-methyl cellulose were provided as carbon sources. After 28 days of growth the highest decrease of nitrocellulose was observed with Chaetomium elatum when up to 43% was degraded in a medium containing nitrocellulose as the only nitrogen source. Coprinus cinereus caused a 37% decrease of nitrocellulose when provided with amino acids and starch as co-substrate. In cultures of Trametes versicolor, Pleurotus ostreatus and Trichoderma reesei, only 10%-22% decrease of nitrocellulose was measured in all media. In the presence of nitrocellulose with N content below 12% supplied as 3 mm pellets as the only carbon source, or with nitrocellulose with carboxy-methyl cellulose, the release of nitrite and nitrate from liquid cultures of Chaetomium elatum was measured. Between 6 and 9 days of growth in these media, an increase in both nitrite and nitrate was observed with a loss in weight of nitrocellulose up to 6% achieved after 34 days. The physical nature of the NC pellets may have reduced the rate of degradation in comparison with supplying NC in solution in the cultures.

Biodegradation, Environmental↗

Membrane filtration - atomic absorption spectrometry combination for copper, cobalt, cadmium, lead and chromium in environmental samples.

Cellulose nitrate membrane filter was used for the preconcentration-separation of Cu, Co, Cd, Pb and Cr ions. The analyte ions were collected on the membrane filter by the aid of carmine. Then membrane filter was dissolved by using nitric acid. The levels of the analytes in the final solutions were determined by flame atomic absorption spectrometry (FAAS). The analytical parameters including pH, amounts of carmine, sample volumes etc. have been optimized. No influences have been observed from the matrix ions. The detection limits for analytes were in the range of 0.08 microg/l-0.93 microg/l. The validation of the procedure was checked by the analysis of standard reference sediment (GBW 07309). The present method has been successfully applied for the FAAS determinations of analyte ions in real samples including black tea and magnesium salts.

Collodion↗

Sodium dodecyl sulfate-mediated transfer of electrophoretically separated DNA-binding proteins.

A modified procedure for the transfer of electrophoretically-separated proteins from sodium dodecyl sulfate (SDS)-polyacrylamide gels onto nitrocellulose filters has been developed. During the diffusion mediated transfer, the SDS-protein complexes were maintained and SDS was added to the buffer. This increases the number of polypeptide species bound to the filter thereby giving an accurate replica of the original gel pattern. The immobilization in the gel of certain polypeptides characterized as DNA-binding proteins, which is observed when SDS is eliminated prior to blotting is avoided. The molecules blotted in the presence of SDS remain immunoreactive and able to bind DNA.

Animals↗

Efficient transfer of proteins from acetic acid-urea and isoelectric-focusing gels to nitrocellulose membrane filters with retention of protein antigenicity.

A method which facilitates the rapid and quantitative electrophoretic transfer of proteins from gels not containing sodium dodecyl sulfate (SDS) to nitrocellulose membranes is described. The equilibration of non-SDS-polyacrylamide gel electrophoretic gels in a buffer containing SDS confers a net negative charge to the proteins present, presumably as a result of the formation of SDS-protein complexes. Proteins from gels equilibrated in the SDS buffer and then electroblotted in a Tris-glycine buffer at pH 8.3 are transferred with much greater efficiency than are proteins from untreated gels. The method has been shown to significantly enhance the electrophoretic transfer of polyoma viral proteins resolved in either acetic acid-urea or isoelectric-focusing gels to nitrocellulose membranes, and it is suggested that the method should have universal applicability to all gel electrophoresis systems currently employed. The proteins from isoelectric-focusing gels treated with SDS and transferred to nitrocellulose membranes were found to retain antigenicity to antisera prepared against either denatured or native viral proteins.

Acetates↗

India ink staining of proteins on nitrocellulose paper.

India ink staining of proteins that have been electrotransfer blotted onto nitrocellulose paper is described. This stain proved to be a useful adjunct to the enzyme-linked immunoelectrotransfer blot technique. It is more sensitive than Coomassie blue, amido black, and fast green stains and is simple to use.

Animals↗