• Journal of the Korean Chemical Society
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• v.28 no.3
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• pp.185-193
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• 1984

At the spermine concentration to cover the number of the binding site of spermine 0.016 per nucleotide, the Hill coefficient of the ethidium binding to the calf thymus DNA was 1.7, while the value was 0.38 in the absence of the spermine. On the basis of the data, together with other present data on the viscometric titration of the DNA with spermine and anomalous absorbance-temperature profile at 260nm and viscosity-temperature profile, it can be speculated that allosteric propagation of the conformational transition induced by the binding of the spermine may be involved in the monomolecular collapse of the DNA to a condensed structure.

• YAKHAK HOEJI
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• v.25 no.4
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• pp.161-165
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• 1981

The binding of two cephalosporins, cephalothin and cefazoline to human serum albumin(HSA) was studied by difference spectrophotometry using a spectrophotometric probe, 2-(4'-hydroxybenzeneazo) benzoic acid. The probe is strong visible absorbing material which interacts with serum albumin to give characteristic spectrophotometric peaks and provides the basis for a convenient assay to measure free and bound amounts in the presence of serum albumin and competitive drugs. The results obtained showed that the probe and cephalosporin compete for the same binding site on human serum albumin; thus the probe can be used to gauge the displacement of cephalosporins from human serum albumin. The data were interpreted on the basis of theory of multiple equilibria. The number of binding sites of human serum albumin for 2-(4'-hydroxybenzeneazo) benzoic acid(HBAB), cephalothin and cefazoline appears to be 4. By using this technique the binding constants were found as follows: HSA-HBAB, $7.89{\times}10^{4}M^{-1}$; HSA-cephalothin, $1.09{\times}10^{3}M^{-1}$ ; HSA-cefazoline, $1.21{\times}10^{3}M^{-1}$.

• Korean Journal of Animal Reproduction
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• v.18 no.2
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• pp.95-99
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• 1994

The purpose of the present study was to determine the in vivo effect of oxytocin antagonist-I(Al) on uterine oxytocin receptor number (Rn) and/or binding affinity (Kd) in the estrous rat. Anesthetized rats were given a bolus infusion of control or 5${\mu}\textrm{g}$ of AI and sacri-ficed 0.5 and 4 hours later. The uterine tissue was removed, trimmed and frozen. Membrane oxytocin receptors were isolated after homogenization of uterine tissue and differential ultracentrifugation. The oxytocin receptor assay was performed by saturation with cold oxytocin competion with a high specific activity oxytocin antagonist. Rn and Kds were determined by nonlinear curve fitting methods. No differences(p>0.05) between the AI and control treated animals in either oxytocin receptor number or binding affinity was detected in this study. These data suggest that the major mode of action of AI is via competitive inhibition at the uterine oxytocin receptor and not by altering receptor number or binding affinity.

• Molecules and Cells
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• v.43 no.7
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• pp.607-618
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• 2020

microRNAs (miRNAs) are non-coding RNA molecules involved in the regulation of gene expression. miRNAs inhibit gene expression by binding to the 3' untranslated region (UTR) of their target gene. miRNAs can originate from transposable elements (TEs), which comprise approximately half of the eukaryotic genome and one type of TE, called the long terminal repeat (LTR) is found in class of retrotransposons. Amongst the miRNAs derived from LTR, hsa-miR-3681 was chosen and analyzed using bioinformatics tools and experimental analysis. Studies on hsa-miR-3681 have been scarce and this study provides the relative expression analysis of hsa-miR-3681-5p from humans, chimpanzees, crab-eating monkeys, and mice. Luciferase assay for hsa-miR-3681-5p and its target gene SHISA7 supports our hypothesis that the number of miRNA binding sites affects target gene expression. Especially, the variable number tandem repeat (VNTR) and hsa-miR-3681-5p share the binding sites in the 3' UTR of SHISA7, which leads the enhancer function of hsamiR-3681-5p to inhibit the activity of VNTR. In conclusion, hsa-miR-3681-5p acts as a super-enhancer and the enhancer function of hsa-miR-3681-5p acts as a repressor of VNTR activity in the 3' UTR of SHISA7.

• The Korean Journal of Pharmacology
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• v.20 no.2
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• pp.23-34
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• 1984

To investigate diurnal variations of opiate receptor binding and its modification by experimental condition or treatment of various centrally-acting drugs, the amount of maximum $^3H-morphine$ binding in rat midbrain homogenates was measured at 4 hour intervals for 24 hours. Animals were conditioned under the controlled L : D, 12 : 12 cycle or D: D, 12 : 12 cycle, for 3 weeks and treated with 0.5 ml of physiological saline or drugs for 2 weeks. A highly significant diurnal rhythm with peak at 22 hour of early dark phase with an amplitude$(0.68{\pm}0.06\;pmole/mg\;protein)$ of +51.1% and nadir $(0.33{\pm}0.03\;mole/mg\;prtein)$ at 18 hour of late light phase with an amplitude of -26.6% was found in control group. 24 tour mean of $^3H-morphine$ binding was $0.45{\pm}0.03\;pmole/mg$ protein respectively. Constant dark adaptation or treatment of reserpine, pargyline, imipramine, amphetamine and chlorpromazine modified the diurnal rhythm in the time of peak and nadir binding shape, phase, amplitude of the diurnal curve and 24 hour mean of $^3H-morphine$ binding. However, Kd values were not changed in all experimental groups : Statistical analysis at times of least and great binding indicates that the differences in $^3H-morphine$ binding were due to changes not in the affinity, but in the number of binding sites. The results are interpreted with regard to the diurnal rhythm of opiate receptor finding. The modes of action of psychoactive drugs are closely related to postulated changes of receptor sensitivity in neuropharmacological aspects.

• BMB Reports
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• v.36 no.2
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• pp.149-153
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• 2003

The dibucaine number (DN) was determined for serum cholinesterase (EC 3.1.1.8, SChE) in plasma samples. The ones with a DN of 79-82 were used, because they had the "usual" SChE variant. The enzyme was assayed colorimetrically by the reaction of 5,5'-dithiobis-[2-nitrobenzoic acid] (DTNB) with the free sulfhydryl groups of thiocholine that were produced by the enzyme reaction with butrylthiocholine (BuTch) or acetylthiocholine (AcTch) substrates, and measured at 412 nm. Dibucaine, a quaternary ammonium compound, inhibited SChE to a minimum within 2 min in a reversible manner. The inhibition was very potent. It had an $IC_{50}$ of $5.3\;{\mu}M$ with BuTch or $3.8\;{\mu}M$ with AcTch. The inhibition was competitive with respect to BuTch with a $K_i$ of $1.3\;{\mu}M$ and a linear-mixed type (competitive/noncompetitive) with respect to AcTch with inhibition constants, $K_i$ and $K_I$ of 0.66 and $2.5\;{\mu}M$, respectively. Dibucaine possesses a butoxy side chain that is similar to the butryl group of BuTch and longer by an ethylene group from AcTch. This may account for the difference in inhibition behavior. It may also suggest the existence of an additional binding site, other than the anionic binding site, and of a hydrophobic nature.

• Archives of Pharmacal Research
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• v.16 no.4
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• pp.305-311
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• 1993

$Na^+,K^+$-ATPase activity, $Na^+$-dependent phosphorylation, and $[^3H]$ ouabain binding in sarcolemma prepared from 4 week old spontaneously hypertensive rat(SHR) ventricles were compared to the same parameters in sarcolemma from age matched nomotensive Wister-Kyoto (WKY) rat ventricles to examine whether the reduced myocardial $Na^+$-pump activity in SHR is an inherited enzymatic defect or a second phenomenon due to sustained hypertension. The total body weights, ventricular weights, and blood pressures were the same for SHR and WKY. No significant differences in sarcolemmal protein content and protein recovery were noted between the two groups. Sarcolemma isolated from SHR ventricles showed significantly less $Na^+,K^+$-ATPase activity ande number of phosphorylation sites when compared to sarcolemma from the WKY ventricles. Equilibrium binding of $[^3H]$ouabain and the tumover number of myocardial $Na^+,K^+$-ATPase, however, were the same for both groups. These reults indicate that the low affinity $(\alpha,\;or\;\alpha^1)\;\alpha$ isoform is the same in ventricles of SHR and WKY. The reduced amount of isoform of the $Na^+,K^+$-ATPase inprehypetensive SHR ventricles may play some role in the development of hypertension.

• Journal of Life Science
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• v.4 no.3
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• pp.92-101
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• 1994

With the rapid development of bioorganic chemistry recently, a field of artificial enzymes has a great concern from the industrial point of view. A number of possibilities now exist ofr the construction of artificial enzymes. They must posses two structural entities, a substrate-binding site and a catalytically effective site. It has been found that producing the facility for substrate binding is relatively straightforward but catalytic sites are somewhat more difficult. Therefore, synthetic catalysts do not yet match all the properties of an enzyme, however, the design of catalysts has lead to very powerful effects. This article reviews the existing literature on the modeling of artificial enzymes using cyclodextrin, modified cyclodextrin and crown compounds.

• Journal of KIISE:Computer Systems and Theory
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• v.29 no.9
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• pp.493-502
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• 2002

The connectivity and edge-connectivity have been the prime deterministic measure of fault tolerance in multicomputer networks. These parameters have a problem that they do not differentiate the different types of disconnected graphs which result from removing the disconnecting vertices or disconnecting edges. To compensate for this shortcoming, one can utilize generalized measures of connectedness such as superconnectivity, toughness, scattering number, vertex-integrity, binding number, and restricted connectivity. In this paper, we analyze such deterministic measures of fault tolerance in recursive circulants and hypercubes, and compare them in terms of fault tolerance.

• YAKHAK HOEJI
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• v.30 no.1
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• pp.42-46
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• 1986

The binding characteristics of five cephalosporins, cefamandole, ceftriaxone, cefoxitin, latamoxef, and cefotetan to bovine serum albumin (BSA) was examined by UV difference spectrophotometry. 2-(4'-hydroxybenzeneazo) benzoic acid was used as the spectrophotometric probe. Competitive bindings between the probe and cephalosporins were observed. Based on the Scatchard plot, the BSA appeared to have two classes of binding sites in BSA binding with cephalosporins. The number of primary binding sites appears to be one, secondary binding sites appears to be three. The binding constants were found as follows: BSA-HBAB; $K_1^{obs}$=8.39$\times$$10^4$ $M^{-1}$, $K_2^{obs}$=1.60$\times$$10^4$ $M^{-1}$, BSA-Cefamandole; $K_1^{obs}$=5.44$\times$$10^3$ $M^{-1}$, $K_2^{obs}$=0.74$\times$$10^3$ $M^{-1}$, BSA-Cefotriaxone; $K_1^{obs}$=6.78$\times$$10^3$ $M^{-1}$, $K_2^{obs}$=0.88$\times$$10^3$ $M^{-1}$, BSA-Cefoxitin; $K_1^{obs}$=7.24$\times$$10^3$ $M^{-1}$, $K_2^{obs}$=1.13$\times$$10^3$ $M^{-1}$, BSA-Latamoxef; $K_1^{obs}$=8.87$\times$$10^3$ $M^{-1}$, $K_2^{obs}$=1.92$\times$$10^3$ $M^{-1}$, BSA-Cefotetan; $K_1^{obs}$=15.41$\times$$10^3$ $M^{-1}$, $K_2^{obs}$=2.7$\times$$10^3$ $M^{-1}$.