• Korean Journal Plant Pathology
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• v.13 no.1
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• pp.1-4
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• 1997

Viroid-like RNA molecules were detected from the low molecular weight RNAs isolated from the Korean peonies which showed typical viroid symptoms of epinasty and dwarfing. Low molecular weight RNAs including viroid RNA molecules were purified by the Qiagen anion exchange minicolumns. Viroid-like RNA molecules showed a single viroid specific band in the native polyacrylamide gel. They were separated into two bands in the denaturing gel conditions. The band of circular form of viroid-like RNAs was crossed over the horizontal band of the linear form of viroid-like RNA molecules in 0~8 M urea gradient gel under the denaturing conditions of 37$^{\circ}C$. The two circular forms of viroid-like RNA molecules were detected in the reverse polyacrylamide gel electrophoresis. The viroid-like RNA molecules purified from the peonies were supposed to be unidentified viroid RNA molecules.

• Journal of Microbiology
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• v.34 no.4
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• pp.384-386
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• 1996

Application of polyacrylamide gel (PAG) instead of agar to solid cultures of Streptomyces spp. was studied. The improved media were prepared by 1) gelling 20 ml of 5% acrylamide in a glass petri dish at room temperature, 2) washing by running water for more than 8 hr to remove residual reaction reagents, 3) drying at 5$0^{\circ}C$ for 12 hr to make a gel film, 4) autoclaving at 121$^{\circ}C$ for 15 min, and 5) swelling gel for about 4 hr by adding sterile liquid medium. In PAG media there were no differences from the observation of morphological characteristics showing during the cellular differentiation on agar media, whereas the ability to utilize carbohydrates differed somewhat from agar media. Agar media thus were little favorable for biochemical tests which the growth was determined depending on the formation of colony, but washed PAG was superior to serve as a solidifying agent.

• Korean Journal of Food Science and Technology
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• v.14 no.1
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• pp.1-5
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• 1982

An invertase from Korean ginseng (Panax ginseng C. A. Mayer) was purified by means of DEAE-cellulose column chromatography and gel-filtration through Sephadex G-75. The homogeneity of the purified invertase was proved by polyacrylamide gel disc electrophoresis. The enzyme was separated into two subunits by SDS-polyacrylamide gel electrophoresis, showing its molecular weights as 48,000. The enzyme preparation showed a characteristic protein UV-spectra.

• Korean Journal of Microbiology
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• v.20 no.4
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• pp.183-188
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• 1982

The neurotoxin of Clostridium botulinum type B was purified from a liquid culture. The purification steps consist of ammonium sulfate precipitation of whole culture, treatment of Polymin P(0.15%, v/v), gel filtration on Sephadex G-100 at pH5.6 and DEAE-Sephadex charomatography at pH8.0. The procedure recovered 17% of the toxin assayed in the starting culture. The toxin was homogeneous by sodium dodecyl sulfate(SDS)-polyacrylamide gel electrophoresis and had a molecular weight of 163, 000. Subunits of 106, 000 and 56, 000 molecular weight were found when purified toxin was treated with a disulfide-reducing agent and electro phoresed on SDS-polyacrylamide gels.

• Korean Journal of Plant Resources
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• v.10 no.3
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• pp.258-264
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• 1997

The introduction of molecular biology methodologies to plant improvement programs offers an invaluable opportunity for extensive germplasm characterization. We have applied the developed technique of random amplification of polymorphic DNA(RAPD)to the analysis of evaluating genetic diversity among Korean wild Codonopsis lanceolata. A total of 340 polymorpic hands were gernerated on agarose- and polyacrylamide-gel by 19 primers of abitrary sequence. grouped by cluster analysis using sample matching coefficients of similarity. Among of the samples. the minimum genetic distance value was obtained between sample no. 1(Girisan) and no. 2(Girisan), and the largest value between sample no. 11(Sulaksan) and no. 17(Sulaksan).In separate cluster dendrograms based on agareose - and polyacryamide-gel. some differences were observed; In the case of agarose gel,41 samples could be devided into 7 groups at below about 0.44 level of distance. However they were divided into 6 gourps at below about 0.40 level of distance in the case of polyacrylamide gel. These results showed that polymophic data in agrose were not grouped to wild plant selected from each mountainous district except for wild plants selected from Sulaksan and Chiaksan. We believe that polyacrylamide-RAPD is a superior method for detecting DNA polymorphism compared to agarose-RAPD method.

• Archives of Pharmacal Research
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• v.25 no.5
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• pp.704-708
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• 2002

A fast and sensitive protein staining method in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) using both an acidic dye, Coomassie Brilliant Blue R-250 (CBBR) and a basic dye, Neutral Red (NR) is described. It is based on a counter ion-dye staining technique that employs oppositely charged two dyes to form an ion-pair complex. The selective binding of the free dye molecules to proteins in an acidic solution enhances the staining effect of CBBR on protein bands, and also reduces gel background. It is a rapid staining procedure, involving fixing and staining steps with short destaining that are completed in about 1 h. As the result, it showed two to fourfold increase in sensitivity comparing with CBBR staining. The stained protein bands can be visualized at the same time of staining.

• Applied Biological Chemistry
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• v.27 no.2
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• pp.73-78
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• 1984

The optimum culture time and initial pH, for the production of exo-maltotetraohydrolase from Pseudomonas stutzeri IAM 12097, in the trypticase medium were 36 hrs and pH 6.3, respectively. Exo-maltotetraohydrolase was purified by $(NH_4)_{2}SO_4$ and two times of column chromatography on DEAE-cellulose. Specific activity of the purified enzyme was 108.6U/mg protein and yield of the enzyme activity was 9.4%. The purified enzyme showed a single band on polyacrylamide gel electrophoresis and SDS-polyacrylamide gel electrophoresis.

• Biotechnology and Bioprocess Engineering:BBE
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• v.6 no.3
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• pp.179-182
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• 2001

Porcine liver esterase was immobilized in polyacrylamide gel for the enantioselective production of levofloxacin from ofloxacin butyl ester. The initial activity of immobilized esterase was found to be significantly affected by the polyacrylamide gel composition. The optimum concentrations of monomer and crosslinker were determined to be 20% and 8.3%, respectively. The activity of immobilized esterase was 55.4% compared to a free enzyme. Enantiomeric excess was maintained at 60%, almost the same level as that of free enzyme. In addition, the immobilized esterase could be used repeatedly up to 10 times without experiencing any severe loss of activity and enantioselectivity.

• Korean Journal of Food Science and Technology
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• v.18 no.3
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• pp.173-180
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• 1986

To investigate on the biochemical characteristics of muscle fiber, myofibrils and actomyosins were prepared front red muscle and white muscle, and their ATPase activities and SDS-polyacrylamide gel electrophoretic patterns were compared. Also biochemical characteristics of bovine muscle were compared with those of chicken muscle for the detection of species characteristics. SDS-polyacrylamide gel electrophoretic analysis indicated that red muscle contained nlore 30K component of myofibril than white muscle. Differences in KCI concen-tration dependency of actomyosin ATPase activities and ATPase activity-pH cone were observed, when bovine muscle were compared with chicken muscle.

• Microbiology and Biotechnology Letters
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• v.16 no.6
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• pp.438-442
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• 1988

The enzyme produced by Rhizopus japonicus was able to convert selectively ginsenoside-Rb$_1$which is the most abundant ginseng saponin, into ginsenoside-Rd which was known to be superior to ginsenoside-Rb$_1$pharmaceutically. The convertible enzyme was purified homogeneous from wheat bran culture of Rhizopus japonicus by ammonium sulfate fractionation and column chromatography of TEAE-cellulose, DEAE-Sephadex A-50, Sephadex G-150, Sepharose 2B. Specific activity of the purified enzyme was increased to a bent 96 folds and yield was appeared to be 11% of culture extract. Evidence for homogenity was obtained from polyacrylamide and SDS-polyacrylamide gel electrophoresis. Molecular weight of the enzyme was estimated about 88, 000 daltons by Sephadex G-l50 gel filtration and SDS-polyacrylamide gel electrophoresis, and it did not consist of any subunit.