• Molecules and Cells
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• v.25 no.1
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• pp.86-90
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• 2008

Caspase-3 (CASP3) plays a key role in apoptosis. In this study, HAX-1 was identified as a new substrate of CASP3 during apoptosis. HAX-1 was cleaved by CASP3 during etoposide-(ETO) induced apoptosis, and this event was inhibited by a CASP3-specific inhibitor. The cleavage site of HAX-1, at $Asp^{127}$, was located using N-terminal amino acid sequencing of in vitro cleavage products of recombinant HAX-1. Overexpression of HAX-1 inhibited ETO-induced apoptotic cell death. It also inhibited CASP3 activity. Together, these results suggest that HAX-1, a substrate of CASP3, inhibits the apoptotic process by inhibiting CASP3 activity.

• Journal of Microbiology and Biotechnology
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• v.28 no.9
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• pp.1473-1481
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• 2018

A cellulase hyperproducing mutant strain, JNDY-13, was obtained using the ARTP mutation system and with Trichoderma reesei RUT-C30 as the parent strain. Whole-genome sequencing of JNDY-13 confirmed that 105 of the 653 SNPs were point mutations, 336 mutations were deletions and 165 were insertions. Moreover, 99 mutations were insertions and duplications. Among all the mutations, the one that occurred in the galactokinase gene might be related to the production of cellulases in T. reesei JNDY-13. Moreover, the up-regulation of cellulase and hemicellulase genes in JNDY-13 might contribute to higher cellulases production. Under optimal conditions, the highest cellulase activity by batch fermentation reached 4.35 U/ml, and the highest activity of fed-batch fermentation achieved was 5.40 U/ml.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.45 no.2
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• pp.114-121
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• 2012

A novel neuropeptide was isolated from the skin of the snakehead Channa argus using the dorsal retractor muscle (DRM) of a starfish Asterina pectinifera as a bioassay system. The amino acid sequence of the purified peptide was analyzed using automated sequencing and MALDI-TOF mass spectrophotometry. The primary structure of the purified peptide was determined to be Pro-Ala-Leu-Ala-Leu. To investigate the complete primary structure of this peptide, Pro- Ala-Leu-Ala-Leu-OH and Pro-Ala-Leu-Ala-Leu-NH2 were synthesized. The chemical and pharmacological properties of the synthetic peptides were compared with those of the native peptide. Both the native peptide and synthetic Pro-Ala- Leu-Ala-Leu-OH had identical behaviors on the reverse-phase and cation-exchange HPLC chromatograms. Synthetic Pro-Ala-Leu-Ala-Leu-OH showed contractile activity on the DRM, and the threshold concentration of this peptide was approximately $10^{-8}$ M. The maximal contractile effect ($E_{max}$) of this peptide was $294{\pm}45.4$% at $10^{-5}$ M.

• Journal of Microbiology and Biotechnology
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• v.20 no.2
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• pp.370-374
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• 2010

A gene encoding the major secreted fibrinolytic protein of Bacillus amyloliquefaciens CH86-1 was cloned from genomic DNAs. DNA sequencing showed that the gene, aprE86-1, could direct the synthesis of a mature protein 275 amino acids in length after processing. When aprE86-1 was introduced into B. subtilis, a mature 27-kDa protein was produced as expected. The fibrinolytic activity of the B. subtilis transformant (TF) was higher than that of B. amyloliquefaciens CH86-1, showing the possibility of increasing the fibrinolytic activity of Bacillus strains through genetic engineering.

• BMB Reports
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• v.37 no.5
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• pp.574-581
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• 2004

The full-length cDNA of the lumbrokinase fraction 6 (F6) protease gene of Lumbricus rubellus was amplified using an mRNA template, sequenced and expressed in E. coli cells. The F6 protease gene consisted of pro- and mature sequences by gene sequence analysis, and the protease was translated and modified into active mature polypeptide by N-terminal amino acid sequence analysis of the F6 protease. The pro-region of F6 protease consisted of the 44 residues from methionine-1 to lysine-44, and the mature polypeptide sequence (239 amino acid residues and one stop codon; 720 bp) started from isoleucine-45 and continued to the terminal residue. F6 protease gene clones having pro-mature sequence and mature sequence produced inclusion bodies in E. coli cells. When inclusion bodies were orally administrated rats, generated thrombus weight in the rat' venous was reduced by approximately 60% versus controls. When the inclusion bodies were solubilized in pepsin and/or trypsin solutions, the solubilized enzymes showed hemolytic activity in vitro. It was concluded the F6 protease has hemolytic activity, and that it is composed of pro- and mature regions.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.45 no.4
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• pp.358-366
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• 2012

A novel neuropeptide was isolated from the skin of the conger eel Conger myriaster using hagfish Eptatretus burgeri intestine as a bioassay system. The sequence of the purified peptide was analyzed using automated amino acid sequencing and MALDI-TOF mass spectrophotometry. The molecular ion peak in the MALDI-TOF mass spectrum of the peptide was at m/z 962.89 $(M+H)^+$. The sequence of the peptide was determined to be L-P-M-L-E-T-Q-M, and was tentatively named comyrin. To investigate the complete primary structure of comyrin, comyrin-OH and comyrin-$NH_2$ were synthesized and the chemical and pharmacological properties of the synthetic peptides were compared with those of the native peptide. However, the elution time of synthetic peptides did not match that of the native peptide on the reverse-phase HPLC chromatogram. In addition, the synthetic peptides did not cause contractile activity in the intestinal smooth muscle of the hagfish. Based on these results, one possible reason for this disagreement may be the presence of a D-amino acid in comyrin.

• Preventive Nutrition and Food Science
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• v.4 no.1
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• pp.28-32
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• 1999

A novel antimicrbial peptide , named HFS-I, was isolated and characterized from the skin of the hagfish, Eptatretus bugeri. The decapeptide with a molecular mass of 1279.5 Da was purified to homogeneity using a gel-filtration column, ion-exchange and C18 reverse-phase high performance liquid chromatograpy . The complete amino acid sequence of HFS-I, which was determined by a combination of an automated amino acid sequencing and FAB-MS, was F-P-W-W-L-S-G-K-Y-P-NH2. Comparison of the amino acid sequence with those of other known antimicrobial peptides revealed that HFS-I was a novel antimicrobial peptide. HFS-I showed a weak antimicrobial activity in vitro aganinst a broad spectrum of microorganism without hemolytic acitivity.

• Microbiology and Biotechnology Letters
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• v.24 no.4
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• pp.472-477
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• 1996

Natural human epidermal growth factor (nhEGF) was purified from pregnant human urine by benzoic acid adsorption, DEAE-Sepharose ion exchange, and immunoaffinity chromatography. The purified nhEGF was further separated into four fractions using Bondapak C$_{18}$ HPLC system. Following characterization by Western blot analysis and double immu- nodiffusion, we found that each fraction corresponds to four derivatives of the nhEGF. For biological analysis of nhEGF, we optimized the labeling time and serum concentration for the incorporatioin of 5-bromo-2'-deoxy uridine (BrdU), a non-radioactive alternative for [$^{3}$H]-thymidine uptake, into NIH 3T3 cells. The DNA synthesis of NIH 3T3 cells was gradually increased at the nhEGF concentrations between 0.1 - 10 ng/ml in the Dulbecco's Modified Eagles Medium (DMEM) containing 0.2% Fetal calf serum (FCS). When we assayed the biological activity of four fractions, the activity of the second fraction was superior to that of the others. Based on the results from the HPLC analysis spiked with recombinant human epidermal growth factor (rhEGF) and amino acid sequencing, we concluded that the second fraction was nhEGF and the other three fractions were the derivatives of nhEGF. In addition, the proportion of nhEGF was approximately 46% is compared with that of the other three derivatives.

• Biotechnology and Bioprocess Engineering:BBE
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• v.8 no.3
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• pp.199-204
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• 2003

Among 59 Korean isolated, 20 were confirmed as members of the genus Bifidobaferium species based on gram staining, microscopic examination of cell morphology and the TLC method, The oxygen tolerance and antioxidative activities of these 20 Bifidobacterium strains and 5 standard Bifidobaferium strains were tested. All the strains demonstrated antioxidative activities as regards inhibiting linoleic acid peroxidation. The antioxidative activities of isolated and standard strains were found to range from 10.7-46.4% and from 10.7-22.2%, respectively. In addition, all tested strains exhibited a Scavenging ability on DPPH free radicals, range from 15-41% for the isolated strains and 8.3-22% for the standard strain. Accordingly. the isolated Bifidobarterium strains demonstrated higher antioxidative artivities than the 5 standa rd Bifidobarterium strains. On the base of grades for each test, HJL 7511 was identified 35 the best strain, followed by HJL 7501. 2 strains were identified with Polymerase Chain Reaction (PCR) assay using group-specific primers designed from the nucleotide Sequences of the 16S rRNA and internal transcribed spacer (ITS) regions of the Bifidobacteria. Based on the Sequencing results, HJL 7511 and HJL 7501 were identified as Bifidobacterium infantis.

• Korean Journal of Microbiology
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• v.54 no.2
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• pp.171-173
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• 2018

Enterococcus faecium was commonly used as a probiotics and feed additives to human and animals because of their beneficial effects. We sequenced the genome of E. faecium JB00008 (KACC 92186P) isolated from a Korean fermented soybean paste (Cheonggukjang) that showed antibacterial activity against Escherichia coli. A 2,847,295-bp draft genome was obtained, and it has in 37.84% G + C content in 34 contigs (length, ${\geq}500bp$).