• The Korean Journal of Food And Nutrition
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• v.12 no.5
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• pp.496-501
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• 1999

Albinism is a phenomenon that color of the body surface is changed to white orfaint brown from the specific color to the species by difficiency of pigments due to mutation or disease. This study was undertaken to investigate the experimental basis on the appearance of albinism in cultured flounder Paralichthys olivaceus. The skin and muscle from the normal and albinic flounder were used by measuring contents of amino acid free amino acid. The results were summarized as follows: Contents of amino acid in theskin and muscle are different from normal and albinic flounder. Phenolic and sulfuric amino acids in the skin of normal flounder were 2 times those of albinic ones. Especially tyrosine contents of the skin in normal flounder were 24 times higher than those. Methionine was 26 times higher than those Phenylalanine was 1.6 times higher. In free amino aicd phosphoserine and phosphoethanolamine were a little higher than that ones. The melanin formation of the skin in flounder was affected by substrates such as phenolic amino acid and cofactor such as sulfuric amino acid.

• Journal of Microbiology
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• v.44 no.4
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• pp.461-465
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• 2006

The occurrence of thioredoxin reductase (NAD(P)H: oxidized-thioredoxin reductase, EC 1.6.4.5, TrxR) in five mesophilic species of Deinococcus was investigated by PAGE. Each species possessed a unique TrxR pattern, for example, a single TrxR characterized D. radiopugnans while multiple forms of TrxR occurred in other Deinococcal spp. Most of TrxRs occurring in Deinococcus showed dual cofactor specificity, active with either NADH or NADPH, although the NADPH specific-TrxR was observed in D. radiophilus and D. proteolytic us.

• Proceedings of the Korean Biophysical Society Conference
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• 2002.06b
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• pp.18-18
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• 2002

Nitrogenase, comprised of the MoFe and Fe proteins, catalyzes the reduction of dinitrogen to ammonia at ambient temperature and pressure. The MoFe protein contains two metal centers, the P-cluster (Fe8S7-8) and the FeMo-cofactor (Fe7S9：homocitrate), the substrate binding site. Despite the availability of the crystal structure of the MoFe protein, suprisingly little is known about the molecular details of catalysis at the active site, and no small-molecule substrate or inhibitor had ever been shown to directly interact with a protein-bound cluster of the functioning enzyme, until our electron-nuclear double resonance(ENDOR) study of CO-inhibited nitrogenase.(omitted)

• YAKHAK HOEJI
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• v.48 no.1
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• pp.13-19
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• 2004

A bacterial expression vector for the human foamy virus (HFV) integrase was constructed and expressed in Escherichia coli. By two-step purification using a nickel-chelated column and a SP-sepharose chromatography; the HFV into-grase protein of 43 kDa was purified to near homogeneity, and used to investigate biochemical characteristics of the enzymatic activities, such as endonucleolytic and disintegration activities. Oligonucleotide substrates were specifically and efficiently cleaved by the purifed HFV integrase in the presence of Mn $^{+2}$, but not in the presence of Mg $^{+2}$, indicating that the HFV integrase is not able to use Mg $^{+2}$ as a cofactor Endonucleolytic reaction was almost completed in 60 min at 37 $^{\circ}C$. In addition, the maximum enzymatic activities were observed at 5 mM Mn $^{+2}$ in the buffer of which pH was from 7.0 to 9.0. The endonucleolytic activities were dose-dependently blocked in the addition of baicalein or chicolic acid which is a well-known inhibitor of human immunodeficiency virus integrase.

• Korean Journal of Microbiology
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• v.26 no.1
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• pp.1-5
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• 1988

The esolation and characterization of a new type II restriction endounclease, BamI, from Bacellus macerans ATCC 8244 were described. BmaI endonuclease was partially purified by procedures of ammonium sulfate fractionation, DEAE-cellulose and phosphocellulose chromatographies. This enzume recognized one site on pBR322 DNA, two sites on Bluescribe DNA, three sites on $\lambda$DNA and no site on SV 40 DNA. The same cleavage patterns for vareius DNAs as PvuI indicated that BamI is an isoschisomer of PvuI whose recognition sequence is 5'-CGATCG-3'. The optimal pH for the BmaI endonuclease activity was about 7.0 and optimal NaCl concentration was about 100mM. Manganese ion could partially replace magnesium as a cofactor, but calcium could not at all.

• Journal of Microbiology
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• v.38 no.4
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• pp.250-254
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• 2000

This study confirmed that white rot fungus Irpex lacteus was able to metabolize 2,4,6-trinitrotoluene (TNT) with two different initial transformations. In one metabolic pathway of TNT a nitro group was removed from the aromatic ring of TNT. Hydride-Meisenheimer complexes of TNT (H$\^$-/-TNT), colored dark redo were confirmed as the intermediate in this transformation by comparison with the synthetic compounds. 2,4-Dinitrotoluene as a following metabolic product was detected, and nitrite produced by denitration of H$\^$-/-TNT supported this transformation. In the other TNT pathway, nitro groups in TNT were successively reduced to amino groups via hydroxylamines. Hydroxylamino-dinitrotoluenes and amino-dinitrotoluenes were identified as the intermediates. The activity of a membrane-associated aromatic nitroreductase was detected in the cell-free extract of I. lacteus. This enzyme catalyzed the nitro group reduction of TNT with NADPH as a cofactor, Enzyme activity was not observed in the presence of molecular oxygen.

• Archives of Pharmacal Research
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• v.20 no.6
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• pp.519-524
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• 1997

Steroid $9{\alpha}$-hydroxylase is an enzyme found in nocardioform microorganisms which can utilize steroids as a sole carbon source. After fractional centrifugation of the cell homogenates, the enzyme activity in Nocardia and Rhodococcus was found in cytoplasmic membrane fraction. On the contrary, Mycobacterium had its 9.alpha.-hydroxylation activity in cytosolic fraction. To characterize the enzyme in these microorganisms, several potential inhibitors of 9.alpha.-hydroxylase were tested and the cofactor requirement for the same enzyme was also examined. The inhibitory effect of ferrous ion chelators indicated involvement of iron containing proteins in the 9.alpha.-hydroxylase system. On the other hand, metyrapone, an inhibitor known to be specific for cytochrome P450 interfered with the enzyme in Mycobacterium, but didn't inhibit the enzyme activity in Nocardia and Rhodococcus. While the $9{\alpha}$-hydroxylase system in Nocardia and Rhodococcus required NADPH, NADH was required as an election donor in Mycobacterium.

• Archives of Pharmacal Research
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• v.5 no.2
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• pp.45-52
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• 1982

Staibilization effect of Panax ginseng C. A. Meyer on .betha.-D-Galactosidase inactivation was proved by kinetic studies of thermal inactivation of the enzyme. The water extract Panax ginseng C. A. Meyer showed stabilization activity at minimal concentration of 10ppm. The methanolic extract was purified to obtain ginseng saponins, and two groups of the ginsenosides, i. e. protopanaxadiol and protopanaxatriol were isolated. They also showed a protective effect against the thermal and chemical inactivation of the enzyme; p-chloromercuribenzoic acid and hydroxylamine known as protein modifier greatly inactivated the enzyme but inactivation was significantly balocked by the ginseng component MG$^{2+}$, known as a cofactor, stabilized the enzyme and the poor stabilization effect by it was potentiated by ginseng components.s.

• Clinical and Experimental Pediatrics
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• v.64 no.8
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• pp.393-399
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• 2021

Food allergies and food-induced anaphylaxis are important health problems. Several cofactors modulating the onset of anaphylaxis have been identified. In the presence of cofactors, allergic reactions may be induced at lower doses of food allergens and/or become severe. Exercise and concomitant infections are well-documented cofactors of anaphylaxis in children. Other factors such as consumption of nonsteroidal anti-inflammatory drugs, alcohol ingestion, and stress have been reported. Cofactors reportedly play a role in approximately 30% of anaphylactic reactions in adults and 14%-18.3% in children. Food-dependent exercise-induced anaphylaxis (FDEIA) is the best-studied model of cofactor-induced anaphylaxis. Wheat-dependent exercise-induced anaphylaxis, the most common FDEIA condition, has been studied the most. The mechanisms of action of cofactors have not yet been fully identified. This review aims to educate clinicians on recent developments in the role of cofactors and highlight the importance of recognizing cofactors in food allergies and food-induced anaphylaxis.

• BMB Reports
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• v.52 no.4
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• pp.227-238
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• 2019

GROWTH-REGULATING FACTORs (GRFs) are sequence-specific DNA-binding transcription factors that regulate various aspects of plant growth and development. GRF proteins interact with a transcription cofactor, GRF-INTERACTING FACTOR (GIF), to form a functional transcriptional complex. For its activities, the GRF-GIF duo requires the SWITCH2/SUCROSE NONFERMENTING2 chromatin remodeling complex. One of the most conspicuous roles of the duo is conferring the meristematic potential on the proliferative and formative cells during organogenesis. GRF expression is post-transcriptionally down-regulated by microRNA396 (miR396), thus constructing the GRF-GIF-miR396 module and fine-tuning the duo's action. Since the last comprehensive review articles were published over three years ago, many studies have added further insight into its action and elucidated new biological roles. The current review highlights recent advances in our understanding of how the GRF-GIF-miR396 module regulates plant growth and development. In addition, I revise the previous view on the evolutionary origin of the GRF gene family.