Separation and recovery of nucleic acids with improved biological activity by acid-degradable polyacrylamide gel electrophoresis

2010 ◽  
Vol 31 (10) ◽  
pp. 1656-1661 ◽  
Author(s):  
Yoon Kyung Kim ◽  
Young Jik Kwon
1995 ◽  
Vol 16 (1) ◽  
pp. 903-904 ◽  
Author(s):  
Friederike Hilbert ◽  
Burkhard Mayr ◽  
Fritz Lackner ◽  
Friedrich Bauer

2018 ◽  
Author(s):  
Emerald R. Tayor ◽  
Silvia Cavuoto ◽  
David M. Beal ◽  
Sophie Caujolle ◽  
Adrian Podoleanu ◽  
...  

<p>The prevalence, distinctive reactivity, and biological significance of sulphur-based groups in proteins and nucleic acids means that analysis of sulphur is of prime importance in biochemistry, biotechnology, and medicine. We report steps in the development of a method to detect these moieties using gold nanoparticles as adjuncts in polyacrylamide gel electrophoresis (Gold-PAGE).<b></b></p>


1983 ◽  
Vol 215 (3) ◽  
pp. 697-699 ◽  
Author(s):  
Y S Zhang ◽  
Q P Cao ◽  
Z G Li ◽  
D F Cui

Des-(B25-B30)-hexapeptide-insulin with B23-glycine replaced by D-alanine was prepared by a combination of enzymic and non-enzymic syntheses. The purified product was homogeneous in polyacrylamide-gel electrophoresis and could be crystallized. The biological activity in vivo of crystalline [B23-D-Ala]des-(B25-B30)-hexapeptide-insulin was determined as 58% of that of standard pig insulin (27 i.u./mg).


1973 ◽  
Vol 51 (6) ◽  
pp. 888-895 ◽  
Author(s):  
Cecily Mills ◽  
M. J. Fraser

Three fractions with single-strand-specific nuclease activity have been isolated by chromatography on phosphocellulose and hydroxyapatite from Neurospora crassa conidia. Two of the fractions containing, respectively, 9% and 7% of the total nuclease activity recovered had the same chromatographic and enzymological properties as the endonuclease and exonuclease previously reported. The third fraction, containing 84% of the total nuclease activity recovered, was shown to contain a mixture of single-strand-specific endonuclease and exonuclease activities enzymologically indistinguishable from the activities previously described. The two components of this fraction were resolved by polyacrylamide gel electrophoresis. A fraction with the same chromatographic properties was also isolated from N. crassa mycelia in which single-strand-specific endonuclease, but no exonuclease activity, was detected. The two mycelial endonuclease fractions were enzymologically indistinguishable. The results were shown not to be due to artifacts of chromatography. Different batches of N. crassa conidia have been found to be heterogeneous with respect to contents of endonuclease and exonuclease.


2018 ◽  
Author(s):  
Emerald R. Tayor ◽  
Silvia Cavuoto ◽  
David M. Beal ◽  
Sophie Caujolle ◽  
Adrian Podoleanu ◽  
...  

<p>The prevalence, distinctive reactivity, and biological significance of sulphur-based groups in proteins and nucleic acids means that analysis of sulphur is of prime importance in biochemistry, biotechnology, and medicine. We report steps in the development of a method to detect these moieties using gold nanoparticles as adjuncts in polyacrylamide gel electrophoresis (Gold-PAGE).<b></b></p>


1975 ◽  
Author(s):  
H. Nagasawa ◽  
Y. Hotta ◽  
N. Takara ◽  
M. Fujimaki ◽  
K. Fukutake

After the addition of purified estrogen preparation to the plasma, the anticoagulant activity of antithrombin III measured by Bigg’s method decreases in proportion to the amount of estrogen added. And the biological activity of antithrombin III in the plasma mixed with estrogen decreases proportionally in single immunodiffusion assay with anti-antithrombin III serum. The same findings mentioned above are also observed in the experiences with estron, equilin, equilenin and estradiol.Furthermore, the rocket formation of antithrombin III fraction prepared by Abild-gaard’s method in crossimmunoelectrophresis also disappeares by the addition of estrogen into the reaction mixture, and the electric mobility of antithrombin III fraction with estrogen increases the migration to the anode in polyacrylamide gel electrophoresis.


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