SDS disc electrophoresis of proteins in homogeneous, low-concentrated polyacrylamide gels

2007 ◽  
Vol 28 (10) ◽  
pp. 1508-1513 ◽  
Author(s):  
I. Piotr Maly ◽  
Cordula Nitsch
Keyword(s):  
Disc Electrophoresis ◽  
Polyacrylamide Gels ◽  
Electrophoresis Of Proteins

Characterization of Different Deoxyribonucleases in Human Lymphocytes

1975 ◽  
Vol 30 (11-12) ◽  
pp. 781-784 ◽  
Author(s):  
E. Jürgen Zöllner ◽  
Hans Störger ◽  
Hans-Joachim Breter ◽  
Rudolf Zahn
Keyword(s):  
Human Lymphocytes ◽  
Disc Electrophoresis ◽  
The Other ◽  
Lower Activity ◽  
Nuclear Fraction ◽  
Polyacrylamide Gels ◽  
Cytoplasmic Fraction ◽  
Acid Deoxyribonuclease ◽  
Deoxyribonuclease Activity

Abstract Deoxyribonucleases, Disc Electrophoresis, Lymphocytes Four groups of deoxyribonuclease activities from human lymphocytes have been characterized by deoxyribonuclease assay in DNA-containing polyacrylamide gels following their separation by disc-electrophoresis. All activities hydrolyse DNA endonucleolytically. One neutral deoxyribo­ nuclease found in the cytoplasmic fraction prefers native or UV-irradiated DNA over denatured DNA as substrate and is a 5′-monoester former. Two groups of acid deoxyribonuclease activities are detectable in the nuclear fraction. Both are 3′-monoester formers. One is as well active with denatured DNA as with native DNA, the other one shows the same activity with native and UV-irradiated DNA but lower activity with denatured DNA. An alkaline deoxyribonuclease activity, also localized in the nucleus, is a 5′ -monoester DNA as substrate.

scholarly journals Double-disc Electrophoresis of Proteins

Nature ◽  
1967 ◽  
Vol 213 (5079) ◽  
pp. 922-922 ◽  
Author(s):  
DAVID RACUSEN
Keyword(s):  
Disc Electrophoresis ◽  
Electrophoresis Of Proteins

Analytical electrofocusing and two-dimensional electrophoresis of proteins extracted from the mycelia of aggressive and nonaggressive strains of Ophiostoma ulmi

1986 ◽  
Vol 64 (9) ◽  
pp. 2073-2081 ◽  
Author(s):  
Robert S. Jeng
Keyword(s):  
Dutch Elm Disease ◽  
Two Dimensional ◽  
Polyacrylamide Gels ◽  
Ophiostoma Ulmi ◽  
Two Dimensional Electrophoresis ◽  
Coomassie Blue ◽  
Isoelectric Points ◽  
Additional Protein ◽  
Dimensional Electrophoresis ◽  
Electrophoresis Of Proteins

Soluble mycelial proteins from Ophiostoma ulmi (Buism.) Nannf., the causal agent of Dutch elm disease, were separated by analytical electrofocusing and two-dimensional electrophoresis in polyacrylamide gels. Results showed the aggressive and nonaggressive strains of this pathogen each had about 60 Coomassie blue stained bands having isoelectric points from 3 to 7. Both strains of this fungus had their own characteristic electrofocusing patterns. Nonaggressive isolate S116, for example, lacked two protein bands, one near the anode and one near the cathode, but it had five additional protein bands distributed from pH 4 to 6. Two-dimensional electrophoresis of total soluble proteins depicted that there were 36 proteins found to be specific for the nonaggressive isolate S116 and 12 proteins for the aggressive isolate RR2.

Electrophoresis of Proteins in small Blood-Samples from live Frogs, in 1 mm thick Polyacrylamide Gels

1981 ◽  
Vol 2 (4) ◽  
pp. 315-319
Author(s):  
Harrie E. J. Wijnands
Keyword(s):  
Skeletal Muscle ◽  
Sucrose Solution ◽  
Rana Esculenta ◽  
Polyacrylamide Gels ◽  
Mass Killing ◽  
Protein Patterns ◽  
Genetic Studies ◽  
Blood Samples ◽  
Rana Esculenta Complex ◽  
Electrophoresis Of Proteins

AbstractA method is described that can help preventing the mass killing of frogs when only minute samples oftissue-specificallyblood-are needed, such as for electrophoresis ofproteins in aid ofpopulation genetic studies. About 10 microliter of serum were rather easily collected from the feet, while the animals (belonging to several forms of Rana esculenta complex) stayed relatively unharmed. By means ofvertical electrophoresis in I mm thick polyacrylamide gels several protein patterns were demonstrated in samples as small as I microliter of serum (plus 1 microliter sucrose solution). Patterns of albumin, LDH and esterase could easily be analysed and were compared with literature data. Some more experimenting might result in the production ofgood zymograms ofa-GDH and PHI too. AAT, PGM and CK appeared to be absent in serum but could easily be demonstrated in samples from skeletal muscle.

A study on the degradation of arachin by proteolytic enzymes

1973 ◽  
Vol 51 (11) ◽  
pp. 2217-2222 ◽  
Author(s):  
R. B. van Huystee
Keyword(s):  
Amino Acids ◽  
Proteolytic Activity ◽  
Free Amino Acids ◽  
Free Amino ◽  
Proteolytic Enzymes ◽  
Disc Electrophoresis ◽  
Polyacrylamide Gels ◽  
Macromolecular Protein

The prime purpose of this proteolysis study was to direct attention to alternate means of measuring proteolytic activity other than the determination of free amino acids. The release of peptides from a macromolecular protein during incubation with either papain, pronase, or trypsin was determined by measuring the presence of 280-nm-absorbing molecules in the fractionation range of Sephadex G 25 eluant after incubation. The formation of larger proteinaceous constituents by proteolysis of arachin was analyzed by disc electrophoresis on polyacrylamide gels. Using these techniques it was noted that papain was the most efficient proteolytic agent for the degradation of arachin.

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