• Proceedings of the Korean Fiber Society Conference
• /
• 2003.10a
• /
• pp.43-44
• /
• 2003

The new method for preparing hybrid fibers from aqueous solution is described. The method is based on interfacial polyionic complexation between the counter-charged polymers. Polysaccharides, chitosan and gellan, and polypeptides, poly(L-lysine) and poly(L-glutamic acid) were utilized as the components of the fibers. The chitosan-gellan and poly(L-lysine)-gellan hybrid fibers exhibited a high level biodegradability.

• Proceedings of the Korean Society of Plant Biotechnology Conference
• /
• 2005.04a
• /
• pp.40-40
• /
• 2005

• YAKHAK HOEJI
• /
• v.9 no.3_4
• /
• pp.34-36
• /
• 1965

As the projects of this institute, a hundred and sixtyfive species of plants which are used currently as herb drugs in Korea were screened on the presence of alkaloids, phenolic compounds, flavonoids, chalcones, lactones, glucosides, carbohydrates, terpenoids, steroids proteins, polypeptides, saponins, and organic acids, and the most reliable presence of alkaloids was detected by paper chromatograph. In this paper, presence of alkaloids is added by screening of 45 species.

• YAKHAK HOEJI
• /
• v.8 no.2
• /
• pp.35-36
• /
• 1964

One of projects of this institute is phytochemical survey of the herb drugs in Korea for further study. A hundred and fifteen species of plants which are used currently as herb drugs in Korea were screened on the presence of alkaloids, phenolic compounds, flavonoids, chalcones, lactones, glucosides, carbohydrates, terpenoids, steroids, proteins, polypeptides, saponins, and organic acids, and the most reliable presence of alkaloids was detected by paper chromatography. In this paper, presence of alkaloids is also tabulated after screening other 50 species.

• YAKHAK HOEJI
• /
• v.12 no.3_4
• /
• pp.91-92
• /
• 1968

As the projects of this institute, 280 species of plants which are currently used as herb drugs in Korea were screened on the presence of alkaloids, phenolic compounds, flavonoids, chalcones, lactones, glycosides, carbohydrates, terpenoids, steroids, proteins, polypeptides, saponins, and organic acids, and the most reliable presence of alkaloids detected by thin layer chromatography is added by screening of 75 species.

• YAKHAK HOEJI
• /
• v.13 no.4
• /
• pp.147-148
• /
• 1969

As one of projects of this Institute, 330 species of plants which are currently used as herb drugs in Korea were screened for the presence of alkaloids, phenolic compounds, flavonoids, chalcones, lactones, glycosides, carbohydrates, terpenoids, steroids, proteins, polypeptides, saponins, and organic acids. The most reliable presence of alkaloids detected by thin layer chromatography is presented by screening of 52 species.

• Animal cells and systems
• /
• v.3 no.2
• /
• pp.221-228
• /
• 1999

In order to find a biochemical marker for late Iysosomes, we characterized two cDNAs which were cloned by using a monoclonal antibody (mAb) against Iysosomes in Amoeba proteus as a probe. The two cDNAs, a 1.3-kb cDNA in pBSK-Iys45 and a 1.6-kb cDNA in pBSK-Iys60, were found to encode proteins homologous to pepstatin-insensitive carboxyl proteinases (PICPs). E. coli transformed with pBSK-Iys45 produced two immunopositive polypeptides (45 and 43 kDa) and the cDNA in 1274 bases encoded a 44,733-Da protein (Lys45) of 420 amino acids containing one site for a core oligosaccharide. On the other hand, E. coli transformed with pBSK-Iys60 produced several polypeptides (64, 54, 45, 41, and 37 kDa) reacting with the mAb. The cDNA contained 1629 bases and encoded a 59,231-Da protein (Lys60) of 530 amino acids containing two sites for asparagine-linked core oligosaccharides. These two cDNAs showed identities of 60.3% in nucleotide sequences and 23.6% in amino acid sequences. Lys45 and Lys60 appeared to share XXEFQK as a common antigenic domain. The amino acid sequence of the Lys45 protein showed 17.4% identity and 40.9% similarity to that of PICP from Pseudomonas sp. 101. On the other hand, Lys60 showed a 24.3% identity and 51.9% similarity with human Iysosomal PICP in the amino acid sequence. A putative active center for serine protease, GTS＊xxxxxFxG, was found to be conserved among PICP homologues. The two PICPs are the first reported enzymatic markers for late Iysosomes.

• BMB Reports
• /
• v.38 no.6
• /
• pp.650-660
• /
• 2005

Proteins accumulated in dry, stratified Arabidopsis seeds or young seedlings, totaled 1100 to 1300 depending on the time of sampling, were analyzed by using immobilized pH gradient 2-DE gel electrophoresis. The molecular identities of 437 polypeptides, encoded by 355 independent genes, were determined by MALDI-TOF or TOF-TOF mass spectrometry. In the sum, 293 were present at all stages and 95 were accumulated during the time of radicle protrusion while another 18 appeared in later stages. Further analysis showed that 226 of the identified polypeptides could be located in different metabolic pathways. Proteins involved in carbohydrate, energy and amino acid metabolism constituted to about 1/4, and those involved in metabolism of vitamins and cofactors constituted for about 3% of the total signal intensity in gels prepared from 72 h seedlings. Enzymes related to genetic information processing increased very quickly during early imbibition and reached highest level around 30 h of germination.

• Journal of Microbiology and Biotechnology
• /
• v.17 no.11
• /
• pp.1751-1757
• /
• 2007

Elastin-like polypeptides (ELPs) undergo a reversible inverse phase transition upon a change in temperature. This thermally triggered phase transition allows for a simple and rapid means of purifying a fusion protein. Recovery of ELPs-tagged fusion protein was easily achieved by aggregation, triggered either by raising temperature or by adding salt. In this study, levansucrase has been used as a model enzyme in the development of a simple one-step purification method using ELPs. The levansucrase gene cloned from Pseudomonas aurantiaca S-4380 was tagged with various sizes of ELPs to functionally express and optimize the purification of levansucrase. One of two ELPs, ELP[V-20] or ELP[V-40], was fused at the C-terminus of the levansucrase gene. A levansucrase-ELP fusion protein was expressed in Escherichia coli $DH5{\alpha}$ at $37^{\circ}C$ for 18 h. The molecular masses of levansucrase-ELP[V-20] and levansucrase-ELP[V-40] were determined as 56 kDa and 65 kDa, respectively. The phase transition of levansucrase-ELP[V-20] occurred at $20^{\circ}C$ in 50 mM Tris-Cl (pH 8) buffer with 3 M NaCl added, whereas the phase transition temperature ($T_t$) of levansucrase-ELP[V-40] was $17^{\circ}C$ with 2 M NaCl. Levansucrase was successfully purified using the phase transition characteristics of ELPs, with a recovery yield of higher than 80%, as verified by SDS-PAGE. The specific activity was measured spectrophotometrically to be 173 U/mg and 171 U/mg for levansucrase-ELP[V-20] and levansucrase-ELP[V-40], respectively, implying that the ELP-tagging system provides an efficient one-step separation method for protein purification.

• Korean Journal of Veterinary Research
• /
• v.30 no.3
• /
• pp.297-307
• /
• 1990

To establish an agar-gel immunodiffusion (AGID) test for detection of antibodies to Aujeszky's disease virus(ADV) in swine, the precipitating antigens were prepared by four procedures using the Aujeszky's disease virus, NYJ-1-87 strain isolated from the affected piglets in Korea. The optimal condition for AGID test and the properties of the antigens were investigated. To determine the optimal concentration of antigens, four antigens were experimentally prepared by concentrating the viral fluids by 1/30 to 1/200. It was proved that the antigen precipitated with ammonium sulfate at concentration of 1/100 was the most efficient to detect ADV antibodies by AGID test. When the relationship between the concentration of the antigens and the size of precipitating in radial immunodiffusion test was investigated, a high correlation coefficiency at r=0.95 (y=0.23x+23.4) was estimated, In study on the effects of various buffered salt solutions and agars on the sensitivity of AGID test by using the experimental ADV antigens, it was found that 0.05M tris buffer without sodium chloride at pH 7.2 induced the most distinctive precipitating lines, and that there was no significant differences in the sensitivity between the agarose and Noble's special agar. When the efficiency of AGID test was compared with serum neutralization(SN) test, the sensitivity of AGID test was 100% in SN titer over 1 : 16, 91.7% in SN titer of 1 : 8 and 57.1% in SN titer of 1 : 4. The specificity of AGID test compared with the sera with SN titer under 1 : 2 was 98.4%. Protein analysis of the antigens by SDS-PAGE indicated that antigen I and antigen III showed a specific band of polypeptides with molecular weight of 116 K in comparison with the control antigen. Antigen IV, treated with tween-80 and ammonium sulfate, revealed specific polypeptides bands at the molecular weights 45K, 98K and 150 K.