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김홍겸,이건복 한국공작기계학회 2001 한국공작기계학회 춘계학술대회논문집 Vol.2001 No.-
Generally, main factors of tool damage are cutting speed, feed rate and depth of cut. The increase of those factors can cause tool breakage or worsen product quality such as machining accuracy deterioration. Those three factors are concerned with cutting force. Cutting force reaches at its maximum value when cutter blade cuts away the object directly, and it is the time when tool damages are at high probability. In this study, we detect the maximum cutting force affecting tool damage and control the maximum cutting force based on the measured peak force.
Cloning and Regulation of Schizosaccharomyces pombe Gene Encoding Ribosomal Protein L11
Kim, Hong-Gyum,Lee, Jin-Joo,Park, Eun-Hee,Sa, Jae-Hoon,Ahn, Ki-Sup,Lim, Chang-Jin Korean Society for Biochemistry and Molecular Biol 2001 Journal of biochemistry and molecular biology Vol.34 No.4
The cDNA encoding ribosomal protein was identified from a cDNA library of Schizosaccharomyces pombe. The nucleotide sequence of the 548 by cDNA clone reveals an open reading frame, which encodes a putative protein of 166 amino acids with a molecular mass of 18.3 kDa. The amino acid sequence of the S. pombe L11 protein is highly homologous with those of rat and fruit, while it is clearly less similar to those of prokaryotic counterparts. The 1,044 by upstream sequence, and the region encoding N-terminal 7 amino acids of the genomic DNA were fused into the promoterless $\beta$-galactosidase gene of the shuttle vector YEp357 in order to generate the fusion plasmid pHY L11. Synthesis of $\beta$-galactosidase from the fusion plasmid varied according to the growth curve. It decreased significantly in the growth-arrested yeast cells that were treated with aluminum chloride and mercuric chloride. However, it was enhanced by treatments with cadmium chloride ($2.5\;{\mu}M$), zinc chloride ($2.5\;{\mu}M$), and hydrogen peroxide (0.5 mM). This indicates that the expression of the L,11 gene could be induced by oxidative stress.
Kim Hong-Gyum,Kim Byung-Chul,Kim Kyunghoon,Park Eun-Hee,Lim Chang-Jin The Microbiological Society of Korea 2004 The journal of microbiology Vol.42 No.4
In a previous study, a gst gene was isolated from the fission yeast Schizosaccharomyces pombe. This gene was dubbed gstI, and was characterized using the gstI -lacZ fusion plasmid pYSH2000. In this work, four additional fusion plasmids, pYSHSDl, pYSHSD2, pYSHSD3 and pYSHSD4, were constructed, in order to carry (respectively) 770, 551, 358 and 151 bp upstream regions from the translational initiation point. The sequence responsible for induction by aluminum, mercury and hydrogen peroxide was located in the range between -1,088 and -770 bp upstream of the S. pombe gstI gene. The same region was identified to contain the nucleotide sequence responsible for regulation by Papl, and has one putative Papl binding site, TTACGTAT, located in the range between $-954\~-947$ bp upstream of the gstI gene. Negatively acting sequences are located between -1,088 and -151 bp. These findings imply that the Papl protein is involved in basal and inducible transcription of the gstI gene in the fission yeast S. pombe.
Hong-Gyum Kim,김병철,김경훈,Eun-Hee Park,임창진 한국미생물학회 2004 The journal of microbiology Vol.42 No.4
In a previous study, a gst gene was isolated from the fission yeast Schizosaccharomyces pombe. This gene was dubbed gst I, and was characterized using the gstI-lacZ fusion plasmid pYSH2000. In this work, four additional fusion plasmids, pYSHSD1, pYSHSD2, pYSHSD3 and pYSHSD4, were constructed, in order to carry (respectively) 770, 551, 358 and 151 bp upstream regions from the translational initiation point. The sequence responsible for induction by aluminum, mercury and hydrogen peroxide was located in the range between -1,088 and -770 bp upstream of the S. pombe gst I gene. The same region was identified to contain the nucleotide sequence responsible for regulation by Pap1, and has one putative Pap1 binding site, TTACGTAT, located in the range between -954 ~ -947 bp upstream of the gst I gene. Negatively acting sequences are located between -1,088 and -151 bp. These findings imply that the Pap1 protein is involved in basal and inducible transcription of the gst I gene in the fission yeast S. pombe.
Kim, Su-Jung,Kim, Hong-Gyum,Kim, Byung-Chul,Kim, Kyunghoon,Park, Eun-Hee,Lim, Chang-Jin The Microbiological Society of Korea 2004 The journal of microbiology Vol.42 No.3
Transcriptional regulation of the Schizosaccharomyces pombe y-glutamylcysteine synthetase (GCS) gene was examined using the two GCS-lacZ fusion plasmids pUGCS101 and pUGCS102, which harbor 607 bp and 447 bp upstream regions, respectively. The negatively-acting sequence was located in the -607 - -447 bp upstream region of the GCS gene. The upstream sequence responsible for induction by menadione(MD) and L-buthionine-(S, R)-sulfoximine (BSO) resides in the -607 - -447 bp region, whereas the sequence which codes for nitric oxide induction is located within the -447 bp region, measured from the translational initiation point. Carbon source-dependent regulation of the GCS gene appeared to be dependent on the nucleotide sequence within -447 bp region. The transcription factor Papl is involved in the induction of the GCS gene by MD and BSO, but not by nitric oxide. Induction of the GCS gene occurring due to low glucose concentration does not depend on the presence of Pap1. These data imply that induction by MD and BSO may be mediated by the Pap1 binding site, probably located in the -607 - -447 region, and also that the nitric oxide-mediated regulation of the S. pombe GCS gene may share a similar mechanism with its carbon-dependent induction.
Kim, Ji-Han,Noh, Ha-Young,Kim, Gyum-Heon,Ahn, Su-Jin,Hong, Go-Eun,Kim, Soo-Ki,Lee, Chi-Ho CSIRO Publishing 2017 Animal Production Science Vol. No.
<P>The aim of the present study was to explore the changes in physicochemical and sensory properties of dry-cured ham (from pigs that received a dietary supplement of processed sulfur, PS), as a function of the level of dietary PS. The following three groups were tested: (1) commercial basal feed (control, CON); (2) 0.1% of PS in the control diet (T1); and (3) 0.3% of PS in the control diet (T2). Dry-cured ham from T2 pigs had a higher moisture content and lower fat concentration than did that from the control pigs. Dry-cured ham T1 and T2 samples showed excellent lipid oxidation stability during storage and showed positive aroma scores in comparison with CON samples. Nonetheless, the total microbial plate count of dry-cured ham T1 (or T2) samples was significantly lower than that of CON samples, and volatile basic nitrogen of T1 (or T2) samples was higher than that of CON samples (P < 0.05). Concentrations of total free amino acids and sulfur-containing amino acids of ham T1 or T2 samples were significantly (P < 0.05) higher than those of control samples. Concentrations of polyunsaturated fatty acids of ham T1 and T2 samples were significantly higher than that of CON samples, whereas concentration of saturated fatty acids of CON samples was significantly higher. Thus, dry-cured ham from pigs receiving 0.3% PS in the diet showed the lowest fat concentration, increased nutrient quality and extended shelf life.</P>
A Second Thioltransferase of Schizosaccharomyces pombe Contains Glutathione S-transferase Activity
Kim, Hong-Gyum,Park, Eun-Hee,Lim, Chang-Jin Korean Society for Biochemistry and Molecular Biol 1999 Journal of biochemistry and molecular biology Vol.32 No.6
Two types of the thioltransferase (also called glutaredoxin) have been previously detected in the cytosolic extract of Schizosaccharomyces pombe, a fission yeast. Previously, the one with a smaller molecular mass (14kDa) was purified and characterized. In the present study, the second thioltransferase was purified. The purification procedure included ammonium sulfate fractionation (40-80%), Sephadex G-200 gel filtration, DEAE-cellulose ion-exchange chromatography, Sephadex G-50 gel filtration, and glutathione-agarose affinity chromatography. The purified enzyme showed a single band on SDS-PAGE, and its molecular mass was determined to be 23 kDa. It utilizes various compounds as substrates, including 2-hydroxyethyl disulfide. Interestingly, we found that the purified thioltransferase also contains significant glutathione S-transferase activity.