• Journal of the Korean Society of Tobacco Science
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• v.19 no.1
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• pp.5-10
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• 1997

Three strains of W isolated from tobacco, tomato and Pepper plants in Korea were characterized based on biological response, serological relationship, and peptide mapping of the capsid Proteins. The strains designated as TMV-common, TMV-Pepper, and TMV-tomato could be distinguishable by different visual symptoms on 3 varieties of tobacco, one variety of tomato and Pepper for each among 27 plant specieces. Serological relationships were examined by agar gel double diffusion test. Only traceable or weak reaction was observed in the incompatible antigen-antibody combinations. The Pepper strain, however, showed trace in reaction with other two antisera. Peptide maps of the capsid proteins digested by V8 protease or by trypsin were also distinguishable, suggesting differences in composition and/or sequence of the amino acids among the strains.

• Proceedings of the Ginseng society Conference
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• 1998.06a
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• pp.160-167
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• 1998

Chemical studies of nitrogen compounds of Panax ginseng seem relatively rare, Probably due to the isolation difficulties, subsequently the investigations of biological activities are little. The experimental conditions were established for highly complete extraction of peptides (basic, acidic and neutral) from Panax ginseng. This task was achieved by applying the follow isolation procedure: 1 , the sequential extraction with water, 0.1% TFA in 20% acetonitril and buffer pH 6.5 (water-pyridine-acetic acid 100:3:900) : 2, fractionation by ultrafiltration : 3, n-butanol extraction 4, cation- and anion-exchange chromatography : 5, chromato-electrophoresis. The comparison of red ginseng (xylem Sl pith part) and red ginseng inside white (xylem Sc pith part) was also provided. To analyze the peptide mixture the chromato-electrophoresis method of separation was applied. Optimal conditions for peptides mapping of sample were explored. Our experiments revealed the quantitative difference of peptide between xylem & pith and phloem & cortex part. We have also found the qualitative difference in the composition of polypeptides between normal red ginseng (xylem Sc pith part) and red ginseng inside-white (xylem St pith part)

• Korean Journal of Microbiology
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• v.38 no.2
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• pp.74-80
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• 2002

The purpose of this work was to investigate the characterization and sequence of catechol 1,2-dioxygenase (Cl,2O) purified from Acinetobacter sp. KS-1 which was grown on benzoate as a sole carbon source. Cl,2O demonstrated its enzyme activity to catechol and 4-methylcatechol. The optimum temperature of Cl,2O was $35^{\circ}C$, and the optimal pH was in the range from pH 7.5 to 9.0. $Ag^{+}$, $Hg^{+}$, and $Cu^{2+}$ showed inhibitory effect on the activity of Cl,2O. Molecular weight of the enzyme was determined to approximately 36 kDa by SDS-PAGE and 7-terminal amino acid sequence of Cl,2O was analyzed as $^{1}MNYQQIDALVKQMNVDTAKG^{20}$and exhibited 95% sequence homology with that of Cl,2O from Acinetobacter radioresistens In addition, trypsin digestion and peptide mapping were performed for internal sequencing analysis. Molecular weights of three digested peptide fragments were analyzed as 966.3 Da, 1933.8 Da and 2081.7 Da by MALDI-TOF, which were matched with each internal sequences $^{1}SQSDFNLRR^{9}\, ^{1}HGNRPSHVHYFNSAPGYR^{18}\, ^{1}TIEGPLYVAGAPESVGFAR^{19}$) of. A. radioresistens. PCR product was amplified with the degenerated primers derived from N-terminal and each internal amino acid sequences.

• Korean Journal of Veterinary Research
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• v.32 no.1
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• pp.83-90
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• 1992

Monoclonal antibodies against structural proteins of bovine viral diarrhea virus(BVDV) were derived by classical hybridoma techniques. These antibodies were characterized by serum neutralization, immunoblotting and immunoprecipitation. The neutralizing monoclonal antibody reacted with the 56kd to 54kd(M.W.) viral protein in western blotting and immunoprecipitation analysis. Although there was no neutralizing activity, another monoclanal antibody reacted with the 45kd protein by immunoprecipitation and with both the 45kd and 36kd proteins in immunoblotting analysis. respectively. Densitometer scanning of purified BVDV and the immunopreipitation of whole virus particles with neutralizing monoclonal antibody revealed the presence of more than twelve viral polypeptides. Although no possible precursor form of protein was identified with the neutralizing monoclonal antibody. the presence of intact virion was detected in the infected cell supernatant immediatelty after pulse labeling, indicating rapid translational processing as well as packaging of the virus. The partial peptide mapping of 45kd and 36kd proteins with Staphylococcus aureus V 8 protease showed that these two proteins are related.

• The Korean Journal of Zoology
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• v.32 no.2
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• pp.142-152
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• 1989

We have produced a new monoclonal antibody detecting common acute lymphoblastic leukemia antigen (CALLA) and designated as KP-22. CALIA detected by KP-22 is expressed on the all of the various cefl lines examined including common ALL. Burkitt's lymphoma, human fibroblasts and cultured normal human fibroblasts. However out of cell lines tested, a fraction of J-ALL and all of myelocytic leukemia and all other nonleukemia cell lines except for fibroblast are CALIA negative. Immunoprecipitation of solubilized 125 I-labeled membrane proteins from cultured human fibroblasts and leukemia cell lines with KP-22 revealed a major polypeptide chain with an apparent molecular weight of approximately 100 Kd and 95 Kd, respectively. Even though a microheterogeneity in terms of molecular weight between two CALLAs, the peptide mapping patterns of them &e identical indicating that such a microheterogeneity seems to be partly due to heterogeneous terminal sialic acid compositions added by a posttranslational modification process.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.51 no.1
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• pp.66-72
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• 2006

Spikelet proteins expressed at the young microspore stage in rice were separated and analysed by two-dimensional polyacrylamide gel electrophoresis (2DE). The separated proteins were electro blotted onto a polyvinylidene difluoride (PVDF) membrane, and 50 proteins were analyzed by a gas-phase protein sequencer. The N-terminal amino acid sequences of 20 out of 50 proteins were determined. N-terminal regions of the remaining proteins could not be sequenced because of blocking. The internal amino acid sequences of proteins were determined by sequence analysis of peptides obtained by the Cleveland peptide mapping method. Results revealed the presence of the photosynthetic apparatus at rice young microspore stage. Major proteins identified in this study could be used as a marker for various studies on physiological stresses.

• Korean Journal of Pharmacognosy
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• v.17 no.2
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• pp.134-138
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• 1986

Based on a tracer study, starch phosphorylase was implicated as an agent in the starch synthesis in sweet potato roots. The enzyme was purified from the tissue as a cluster of isozymes with an average mw of 205K (fresh roots) or 159K (roots stored for 3 mon.). On SDS polyacrylamide gel electrophoresis, one large subunit of 98K mw and several small ones of 47${\sim}57K mw were observed. From the mw data and the results of peptide mapping and immunoelectrophoretic blotting using mono- and polyclonal antibodies, it was deduced that a large part of the large subunit was cleaved at the middle part of the peptide chain to give rise to the small subunits, and on storage, the enzyme molecules were further modified by proteolysis. During the course of phosphorylase purification, a proteinaceous inhibitor of the enzyme was isolated. It had a mw of 250K and was composed of 5 identical subunits of 51K mw. In the direction of starch synthesis, the inhibitor showed a noncompetitive kinetics with a Ki of $1.3{\times}10^{-6}\;M$. By immunohistochemical methods, both the enzyme and the inhibitor were located on the cell wall and amyloplast. Crossreacting materials of the inhibitor were present in spinach leaf, potato tuber and rice grain. These findings indicate the wide occurrence of the inhibitor and also imply its possible participation in regulating starch phosphorylase activity in vivo.

• Journal of the Korean Society of Food Science and Nutrition
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• v.19 no.1
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• pp.94-106
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• 1990

사람들이나 동물의 소화관의 상재균으로서 중요한 Lactobacillus acidophilus의 여러균주를 사용하여 세포표면의 성상을 조사하였다. 불리한 세포벽의 negative 염색한 표본을 전자현미경으로 검토한 결과 사용한 21주중 15주는 세포벽외층에 단백질로 구성딘 regular array를 생산하고 있음을 알았다. RA를 구성하는 단백질의 분자량은 41KDa-48KDa이었다 아미노사노성 및 Staphylococcus au-reus V8 protease로 한정분해 후 및 N-chlorosuccini-mide로 부분절단후의 peptide map에서 Johnson등의 분류의 subgroup A-1에 속하는 균주가 생산하는 RA단백질은 불균질하였으나 그외 균주의 RA단백질은 같은 subgroup에 속하고 있어도 불균질하였음을 알았다 따라서 RA단백질은 불균질하였으나 그외 균주의 RA단백질은 같은 subgroup에 속하고 있어도 불균질하였음을 알았다 따라서 RA생산의 유무 및 RA단백질의 분자량측정과 peptide mapping을 행하면 지금까지 행해온 DNA-hybridization과 같은 복잡한 절차를 사용하지 않아도 subgroup A-1의 L. acidophilus가 동정 가능함을 알았다 L acidophilus의 세포표면소수성은 일반적으로 RA를 생산하지 않는 균주보다는 RA를 생사하는 균주에 높은 것이많았다 RA생산균주에 있어서는 RA단백질은 세포표면소수성과 직접관계하고 있는 것은 적었다.

• Journal of Microbiology and Biotechnology
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• v.10 no.5
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• pp.587-594
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• 2000

Monoclonal antibodies against glutamate dehydrogenase (GDH) from Sulfolobus solfataricus were produced and characterized using epitope mapping and biosensor technology, Five monoclonal antibodies raised against S. solfataricus GDH were each identified as a single protein band that comigrated with purified S. solfataricus GDH on the SDS-polyacrylamide gel electrophoresis and immunoblot. Epitope mapping analysis showed that only one subgroup among the antibodies tested recognized the same peptide fragments of GDH. Using the anti-S. solfataricus GDH antibodies as probes, the cross-reactivities of GDHs from various sources were investigated and it was found that the mammalian GDH is not immunologically related to S. solfataricus GDH. The structural differences between the microbial and mammalian GDHs were further investigated using biosensor technology (Pharmacia BIAcore) and monoclonal antibodies against S. solfataricus and bovine brain. The binding affinity of S. solfataricus glutamate dehydrogenase anti-S. solfataricus for GDH ($K_D$=11 nM) was much tighter than that of anti-bovine for GDH ($K_D$=450 nM). These results, together with the epitope mapping analysis, suggest that there may be structural differences between the two GDH species, in addition to their different biochemical properties.

• Journal of the Korean Society of Food Science and Nutrition
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• v.20 no.1
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• pp.35-39
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• 1991

Properties of a protease purified from Neungee[Sarcodon aspratus(Berk, ) S. Ito] have been investigated. The enzyme displays a glycosylated serine protease. The enzyme is able to hydrolyze alanine glycine methionine glutamine and cysteine of N-CBZ and N-t-BOC-L-amino acid derivatibes relatively strongly but splits valine proline and isoleucine derivatives with low affinity which means the enzyme has the broad substrate spectrum toward the amino acids. Interestingly the enzyme was inhibited by bromelain inhibitor. That is the active site environ-ment of the enzyme is believed to be similar to that of bromelain However peptide mapping studies show that the two enzymes have distinct different cleavage sites.