• Title/Summary/Keyword: ${\beta}$-lysine

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Interaction of ${\varepsilon}-L-{\beta}-lysine$ as a Tail Analogy of Tallysomycin-A to a Double Helical DNA Oligonucletide $d(CGCTTCGAAGCG)_{2}$, was investigated by NMR

  • Lee, Chang-Jun;Won, Ho-Shik
    • 한국자기공명학회논문지
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    • 제11권2호
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    • pp.129-137
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    • 2007
  • During the screening of material which has the antimicrobial activity against aminoglycoside-resistant bacteria, A new material ${\varepsilon}-(L-{\beta}-lysine)$ polypeptide from a culture medium of Streptomyces sp.(DWGS2) was isolated, and the structure and the physicochemical properties of the new material were elucidated. The new material was separated by column chromatography of the culture medium using Dowex $1{\times}2$, Silica gel, and Sephadex LH20 etc. The structure and molecular weight were determined with the data of NMR, MALDI mass, and ESI mass experiments. And the monomer obtained by hydrolysis of the new material with 6N-HCI was identified as a $L-{\beta}-lysine(T_2)$, which is a tail of bleomycin. As tail-region analogy, $T_2({\beta}-lysine$ derivatives from streptomyces) interactions with a self-complementary oligonucleotides, $d(CGCTTCGAAGCG)_2$, was investigated by NMR.

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Identification of Critical Residues for Plasminogen Binding by the αX I-domain of the β2 integrin, αXβ2

  • Gang, Jongyun;Choi, Jeongsuk;Lee, Joo Hee;Nham, Sang-Uk
    • Molecules and Cells
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    • 제24권2호
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    • pp.240-246
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    • 2007
  • The ${\beta}2$ integrins on leukocytes play important roles in cell adhesion, migration and phagocytosis. One of the ${\beta}2$ integrins, ${\alpha}X{\beta}2$ (CD11c/CD18), is known to bind ligands such as fibrinogen, Thy-1 and iC3b, but its function is not well characterized. To understand its biological roles, we attempted to identify novel ligands. The functional moiety of ${\alpha}X{\beta}2$, the ${\alpha}X$ I-domain, was found to bind plasminogen, the zymogen of plasmin, with moderate affinity ($1.92{\times}10^{-6}M$) in the presence of $Mg^{2+}$ or $Mn^{2+}$. The ${\beta}D-{\alpha}5$ loop of the ${\alpha}X$ I-domain proved to be responsible for binding, and lysine residues ($Lys^{242}$, $Lys^{243}$) in the loop were the most important for recognizing plasminogen. An excess amount of the lysine analog, 6-aminohexanoic acid, inhibited ${\alpha}X$ I-domain binding to plasminogen, indicating that binding is lysine-dependent. The results of this study indicate that leukocytes regulate plasminogen activation, and consequently plasmin activities, through an interaction with ${\alpha}X{\beta}2$ integrin.

Effect of ion Pairing on the Cellular Transport of Antisense Oligonucleotide

  • Song, Kyung;Kim, Kyoung-Mi;Kim, Jae-Baek;Ko, Geon-Il;Sohn, Dong-Hwan
    • Archives of Pharmacal Research
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    • 제20권5호
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    • pp.438-442
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    • 1997
  • Antisense oligonucleotide represents an interesting tool for selective inhibition of gene expression. However, their low efficiency of introduction within intact cells remains to be overcome. Antisense-$TGF{\beta}$ (25 mer) and antisense-$TGF{\beta}$ (18 mer) were used to study the cellular transport and biological function of antisense oligonucleotide in vitro. Since TGF and TNF play on important role in regulating the nitric oxide production from macrophages, the action of the above antisense oligonucleotides was easily monitored by the determination of nitrite. Poly-L-lysine, benzalkonium chloride and tetraphenylphosphonium chloride were used as polycations, which neutralize the negative charge of antisense oligonucleotide. The production of nitric oxide mediated by .gamma.-IFN in mouse peritoneal macrophage was increased by antisense-TGF.betha. in a dose-dependent manner. Antisense-$TGF{\beta}$ reduced the nitric oxide release from activated RAW 264.7 cells. Significant enhancement in the nitric oxide production was investigated by the cotreatment of poly-L-lysine with antisense-$TGF{\beta}$On the meanwhile, inhibition effect of antisense-$TGF{\beta}$ is not changed by the addition of poly-L-lysine. These results demonstrate that control of expression of $TGF{\beta}$ and TNF.alpha. gene is achieved using antisense technology and the cellular uptake of antisense oligonucleotide could be enhanced by ion-pairing.

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Structural Basis for Recognition of L-lysine, L-ornithine, and L-2,4-diamino Butyric Acid by Lysine Cyclodeaminase

  • Min, Kyungjin;Yoon, Hye-Jin;Matsuura, Atsushi;Kim, Yong Hwan;Lee, Hyung Ho
    • Molecules and Cells
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    • 제41권4호
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    • pp.331-341
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    • 2018
  • L-pipecolic acid is a non-protein amino acid commonly found in plants, animals, and microorganisms. It is a well-known precursor to numerous microbial secondary metabolites and pharmaceuticals, including anticancer agents, immunosuppressants, and several antibiotics. Lysine cyclodeaminase (LCD) catalyzes ${\beta}$-deamination of L-lysine into L-pipecolic acid using ${\beta}$-nicotinamide adenine dinucleotide as a cofactor. Expression of a human homolog of LCD, ${\mu}$-crystallin, is elevated in prostate cancer patients. To understand the structural features and catalytic mechanisms of LCD, we determined the crystal structures of Streptomyces pristinaespiralis LCD (SpLCD) in (i) a binary complex with $NAD^+$, (ii) a ternary complex with $NAD^+$ and L-pipecolic acid, (iii) a ternary complex with $NAD^+$ and L-proline, and (iv) a ternary complex with $NAD^+$ and L-2,4-diamino butyric acid. The overall structure of SpLCD was similar to that of ornithine cyclodeaminase from Pseudomonas putida. In addition, SpLCD recognized L-lysine, L-ornithine, and L-2,4-diamino butyric acid despite differences in the active site, including differences in hydrogen bonding by Asp236, which corresponds with Asp228 from Pseudomonas putida ornithine cyclodeaminase. The substrate binding pocket of SpLCD allowed substrates smaller than lysine to bind, thus enabling binding to ornithine and L-2,4-diamino butyric acid. Our structural and biochemical data facilitate a detailed understanding of substrate and product recognition, thus providing evidence for a reaction mechanism for SpLCD. The proposed mechanism is unusual in that $NAD^+$ is initially converted into NADH and then reverted back into $NAD^+$ at a late stage of the reaction.

과요오드산 산화당에 의한 인공단백질의 조제 메카니즘 (Preparation Mechanism of Glycoprotein by Periodate-oxidized Soluble Starch and Maltooligosaccharides)

  • 안용근
    • 한국식품과학회지
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    • 제31권2호
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    • pp.482-487
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    • 1999
  • 과요오드산으로 산화시킨 당을 유리아미노산과 반응시켜서 ${\alpha}-NH_2$기와 펩티딜리신의 ${\varepsilon}-NH_2$기와 반응하여 결합한 것을 확인하였다. 그래서, 제조한 과요드산-산화당은 단백질 분자 표면의 리신의 ${\varepsilon}-NH_2$기와 Schiff 염기 반응으로 공유결합하여 당단백질을 만드는 것으로 볼 수 있다. 과요드산 산화당으로 변형한 고구마 ${\beta}$-아밀라아제는 C, H는 증가, N은 감소하였다. N말단의 ${\alpha}-NH_2$기는 70% (pentamer), 73% (monomer), ${\varepsilon}-NH_2$기는 33% (pentamer), 26% (monomer)가 산화당과 반응하였다. 페놀-황산법에 의한 총당 정량과 DNP 법으로 분석한 결과, $IO_4$-산화말토헥사오스는 고구마 ${\beta}$-아밀라아제 1몰당 6몰이 결합된 것으로 나타났고, 고구마 ${\beta}$-아밀라아제에 결합된 산화가용성 전분은 효소단백질 대비 13.2% (monomer), 13.5% (pentamer), 산화말토헥사오스는 9.7% (pentamer), 9.3% (monomer)로 나타났다.

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Amino Acid Alterations in the $\beta$- Tubulin of Metarhizium anisopliae That Confer Benomyl Resistance

  • Kim Soon Kee;Shim Hee Jin;Roh Jong Yul;Li Ming Shun;Choi Jae Young;Jin Byung Rae;Boo Kyung Saeng;Je Yeon Ho
    • International Journal of Industrial Entomology and Biomaterials
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    • 제11권1호
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    • pp.37-42
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    • 2005
  • We cloned the $\beta$-tubulin genes from the wild type strain and two benomyl-resistant mutants of Metahizium anisopliae and determined their nucleotide sequences. A $\beta$-tubulin encoding 448-residue protein from wild type M. anisopliae shows strong homology to other $\beta$-tubulins. The coding region is interrupted by four introns. Comparisons of intron position between the M. anisopliae gene and other fungal $\beta$-tubulin genes show considerable positional conservation. The mutations responsible for benomyl resistance were determined in two spontaneous mutants, 8-18 and 8­19. One mutant 8-18 substituted glutamate for aspar­agine at position 33 and lysine for glutamine at position 134. The other mutant 8-19 showed alterations at three positions of $\beta$-tubulin arginine for tryptophan at position 21, lysine for asparagine at position 33, and phenylalanine for leucine at position 240. These data suggest that regions of $\beta$-tubulin containing amino acids 21, 33,134, and 240 interact to form the binding site of benomyl.

시판 조제 분유의 화학적 품질 평가 (Chemical Quality Evaluation of Commercial Infant Formulas)

  • 한정은;홍윤호
    • 한국축산식품학회지
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    • 제21권1호
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    • pp.56-63
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    • 2001
  • In this study, three domestic and one foreign formulas for the infants up to 5 month old were examined to detect chemical changes such as pH, reactive sulfhydryl groups(RSH) content, 5-hydroxymethylfurfral(HMF) content, available lysine content, electrophoresis, and surface color caused by heat treatment for long term storage. In the SDS-polyacrylamide gel electrophoresis, A and B products showed similar pattern, while C product had a clearly distinguishable $\beta$-lacto-globulin band, but in casein, only D product showed a few strong casein band. RSH content, which indicate the extent of whey protein denaturation, ranged from 4.40 to 5.93 mmole/g protein. HMF content. which indicate the extent of Maillard reaction, ranged from 192 to 432 $\mu$mole/100g in formulas. B product showed the highest RSH and HMF content. Available lysine content ranged from 31 to 46 mg/g protein. Among them D product contain the highest available lysine content and others showed no significant difference. In conclusion, the domestic infant formulas showed higher RSH and HMF content than the foreign product and the available lysine content of the domestic products were lower than of the foreign product.

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Estimating total lysine requirement for optimised egg production of broiler breeder hens during the early-laying period

  • Kim, Eunjoo;Wickramasuriya, Samiru Sudharaka;Shin, Taeg Kyun;Cho, Hyun Min;Kim, Hyeun Bum;Heo, Jung Min
    • Journal of Animal Science and Technology
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    • 제62권4호
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    • pp.521-532
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    • 2020
  • The production performance of broiler breeder hens in response to different levels of total lysine during the early laying period was investigated. A total of 126 Ross 308 parent stock hens were offered one of seven dietary treatments formulating elevated contents of total lysine ranging from 0.55% to 0.79% (0.04 scale; 133 g of feed) from 23 to 29 weeks of age. Each treatment had six replicates with three birds per pen. Body weight was recorded triweekly and eggs were collected and weighted at 9:00 am daily. One hen from each pen was euthanized to collect blood samples and visceral organs were harvested and weighed. Egg production, egg weight and egg mass were lower (p < 0.05) in hens offered a diet containing 0.55% total lysine compared to those fed the diet containing higher total lysine. Hens offered a diet containing 0.71%, 0.75%, and 0.79% total lysine had greater (p = 0.008) egg production rate compared to those offered a diet containing lysine less than 0.71%. The number of total eggs produced tended to be greater (p = 0.083) in hens offered a diet containing 0.71 and 0.75% total lysine compared to the other treatments. The number of settable egg production was higher (p < 0.001) in hens offered a diet contacting 0.79% total lysine compared to those fed the diet containing lower levels of total lysine. The relative weights of oviduct and ovary were lower (p < 0.05) in hens offered a diet containing 0.59% total lysine compared to the other treatments. No difference found in body weight, the number of total eggs, double-yolk eggs and abnormal shell eggs among the treatments. The urea nitrogen, estradiol-17 beta and progesterone in plasma were not affected by treatments. Based on linear- and quadratic-plateau models, total lysine requirements for egg production, settable egg production and egg mass at the early laying period were to be 0.73%, 0.77%, and 0.71%, respectively. Modern broiler breeder hens likely require higher total lysine than NRC recommendation in a diet for enhancing productivity during the early-laying period.