• Archives of Pharmacal Research
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• 제12권3호
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• pp.160-165
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• 1989

Binding of sulfaethidole to bovine serum albumin was studied by equilibrium dialysis, fluorescence probe technique, uv difference spectrophotometry and circular dichroism. Equilibrium dialysis method enabled us to estimate the total number of drug binding sites of albumin molecule. For sulfaethidole, albumin had 6 primary and 40 secondary binding sites. The primary and secondary binding constants were 0.9 * 10/sup 5/ M/sup -1/ and 0.2 * 10/sup 6/ M/sup -1/, respectivitely. 1-Anilino-8-naphthalenesulfonate (ANS) and 2-(4-hydroxylbenzeneazo)- benzoic acid (HBAB) were used as the fluorescence probe and the uv spectrophotometric probe, respectively. In fluorescence probe technique, results indicated that the number of higher affinity drug binding site of albumin was 1 and the number of lower affinity drug binding sites of albumin was 3, and the primary and secondary drug binding constants for bovine serum albumin were 2.15 * 10/sup 5/M/sup -1/ and 1.04 * 10/sup 5/ M/sup -1/, respectively. In uv difference spectrophotometry, binding sites were 3 and binding constant was 1.88 * 10/sup 5/M/sup -1/. The above spectrophotometry, binding sites were 3 and binding constant was 1.88 * 10/sup 5/M/sup -1/. The above results suggest that several different methods should be used in ompensation for insufficient information about drug binding to albumin molecule given by only one method.

• 대한수학회보
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• 제45권1호
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• pp.53-57
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• 2008

Let G be a graph, and let a, b, k be integers with $0{\leq}a{\leq}b,k\geq0$. Then graph G is called an (a, b, k)-critical graph if after deleting any k vertices of G the remaining graph of G has an [a, b]-factor. In this paper, the relationship between binding number bind(G) and (a, b, k)-critical graph is discussed, and a binding number condition for a graph to be (a, b, k)-critical is given.

• Journal of applied mathematics & informatics
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• 제25권1_2호
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• pp.339-344
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• 2007

The relationships between binding number and fractional edge (vertex)-deletability or fractional k-extendability of graphs are studied. Furthermore, we show that the result about fractional vertex-deletability are best possible.

• Archives of Pharmacal Research
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• 제27권9호
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• pp.978-983
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• 2004

The effects of glycyrrhizic acid (GLZ) on protein binding of diltiazem, verapamil, and nifedipine were investigated. Protein binding studies (human serum, human serum albumin (HSA) and (X1-acid glycoprotein (AAG)) were conducted using the equilibrium dialysis method with and without addition of GLZ. The binding parameters, such as the number of moles of bound drug per mole of protein, the number of binding sites per protein molecule, and the association con-stant, were estimated using the Scatchard plot. The serum binding of nifedipine, verapamil, and diltiazem was displaced with addition of GLZ, and the decreases of Ks for serum were observed. GLZ decreased the association constants of three drugs for HSA and AAG, while the binding capacity remained similar with addition of GLZ. Although the characteristics of interaction were not clear, GLZ seemed to mainly affect HSA binding of nifedipine rather than AAG binding, while GLZ seemed to affect both AAG- and HSA-bindings of verapamil and dilt-iazem resulting in a serum binding displacement.

• Archives of Pharmacal Research
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• 제7권2호
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• pp.87-93
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• 1984

The effects of ionic strength and pH on the binding of cefazolin to bovine serum albumin (BSA) were studied by UV difference spectrophotometry. As ionic strength at constant pH and temperature increases, the apparent bining constant decreased but the number of binding sites remained almost constant at 2. The constancy of the number of binding sites with increasing the ionic strength suggests that purely electrostatic forces between BSA and drug do not have great importance in the drug binding, even though there is a decrease in the apparent binding constant. Thus, the effect of ionic strength on the interaction between drug and BSA may be explained by the changes in ionic atmosphere of the aggregated BSA molecules and competitive inhibition by phosphate ions. In addition, the higher apparent binding constant at high ionic strength is explained by conformational changes of BSA from its aggregate forms into subunits. The pH effects on the afinity of interactions indicated that the binding affinity of cefazoline is higher in the neutral region than in the alkaline region. An d at high pH value, the number of binding sites decreased from 2 to 1 because of the conformational change of BSA in the alkaline region.

• 한국정보과학회논문지:정보통신
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• 제31권1호
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• pp.27-36
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• 2004

사용자의 이동성을 지원하는 Mobile IP 환경에서, 빈번한 바인딩 갱신 메시지의 발생은 상당한 부하를 초래할 수 있다. 따라서 이를 감소시키기 위한 알고리즘 개발이 필요하다. 이를 위해, 본 논문에서는 사용자의 이동성과 관련된 지역적 특성을 고려한 동적 바인딩 갱신을 위한 라이프타임 할당 기법을 제안한다. 각 이동 노드는 방문한 서브넷과 관련된 로그 정보를 이용하여 프로파일을 유지하고 있다. 즉, 방문한 서브넷별로 평균 상주시간을 기반으로 하여 적응적 라이프타임을 결정하여 다음 방문 시에 이 값을 바인딩 갱신의 라이프타임으로 사용한다. 또한 각 이동 노드가 동일한 서브넷을 방문하더라도 방문 시간대에 따라 평균 상주시간이 차이가 날 수 있다는 사실을 기반으로 하여, 동일한 서브넷에 대하여 방문 시각에 따라 별개의 라이프타임을 결정하는 알고리즘도 제안한다. 제안한 기법의 성능 향상을 보이기 위하여 기존 Mobile IPv6과 비교 실험을 수행하였으며, 이 과정에서 다음의 두 가지 인자를 주로 비교하였다: 바인딩 갱신 메시지의 수 및 바인딩 요청 메시지의 수. 실험 결과, 제안한 기법은 기존 Mobile IPv6에 비해 위 메시지의 수를 줄임으로써 상당한 통신비용 절감효과를 보여주었다.

• Journal of applied mathematics & informatics
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• 제34권5_6호
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• pp.435-441
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• 2016

Let G be a graph, and let g, f be two nonnegative integer-valued functions defined on V (G) with g(x) ≤ f(x) for each x ∈ V (G). A graph G is called a fractional (g, f, n)-critical graph if after deleting any n vertices of G the remaining graph of G admits a fractional (g, f)-factor. In this paper, we obtain a binding number condition for a graph to be a fractional (g, f, n)-critical graph, which is an extension of Zhou and Shen's previous result (S. Zhou, Q. Shen, On fractional (f, n)-critical graphs, Inform. Process. Lett. 109(2009)811-815). Furthermore, it is shown that the lower bound on the binding number condition is sharp.

• Journal of Pharmaceutical Investigation
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• 제19권3호
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• pp.163-171
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• 1989

To investigate the protein binding characteristics of cephalothin, the effects of ionic strength, pH and temperature on the binding of cephalothin to bovine serum albumin (BSA) were studied by UV difference spectrophotometric method. With increasing ionic strength at constant PH and temperature, association constant decreased, but the number of binding sites sites was about 2 constantly. It may be deduced that the binding process is not only due to electrostatic forces. And the increased association constant at high ionic strength is explained by conformational changes of BSA from complex to subunits. The pH effect on the affinity of interaction indicated that the binding affinity of drug is higher in the neutral region than in the alkaline region. And, at high pH value, the number of binding sites decreased from 2 to 1 because of the conformational changes of BSA in alkaline region. The decrease in binding affinity of BSA to drug with increasing temperature was characteristic of an exothermic reaction. And the negative sign of ${\Delta}G^{\circ}$ meant that the binding process occurs spontaneously under the experimental conditions. In cephalothin-BSA complex formation, since the net enthalpy change value and entropy change value are positive, it is assumed that hydrophobic bindings are predominant in this binding process.

• BMB Reports
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• 제31권4호
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• pp.307-327
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• 1998

Cytochrome c peroxidase (CcP) is a yeast mitochondrial enzyme which catalyzes the reduction of hydrogen peroxide to water using two equivalents of ferrocytochrome c. The CcP/cytochrome c system has many features which make it a very useful model for detailed investigation of heme protein structure/function relationships including activation of hydrogen peroxide, protein-protein interactions, and long-range electron transfer. Both CcP and cytochrome c are single heme, single subunit proteins of modest size. High-resolution crystallographic structures of both proteins, of one-to-one complexes of the two proteins, and a number of active-site mutants are available. Site-directed mutagenesis studies indicate that the distal histidine in CcP is primarily responsible for rapid utilization of hydrogen peroxide implying significantly different properties of the distal histidine in the peroxidases compared to the globins. CcP and cytochrome c bind to form a dynamic one-to-one complex. The binding is largely electrostatic in nature with a small, unfavorable enthalpy of binding and a large positive entropy change upon complex formation. The cytochrome c-binding site on CcP has been mapped in solution by measuring the binding affinities between cytochrome c and a number of CcP surface mutations. The binding site for cytochrome c in solution is consistent with the crystallographic structure of the one-to-one complex. Evidence for the involvement of a second, low-affinity cytochrome c-binding site on CcP in long-range electron transfer between the two proteins is reviewed.

• 한국자기공명학회논문지
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• 제20권1호
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• pp.22-26
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• 2016

FANCJ is a DNA helicase which contributes genome stability by resolving G-quadruplex DNA from 5' to 3' direction. In addition to main ATPase helicase core, FANCJ has the protein binding region at its C-terminal part. BRCA1 and BLM are the binding partner of FANCJ and these protein-protein interactions contribute genomic stability and the proper response to replication stress. As the first attempt for studying FANCJ-BLM interaction, we prepared BLM binding region of FANCJ and characterized with CD and NMR spectroscopy. FANCJ (881-941) with N-ter 6xHis was purified as the oligomer. Secondary structure prediction based on CD data revealed that FANCJ (881-941) composed with ${\beta}$ sheet, turn and coils.$^1H-^{15}N$ HSQC spectra showed nonhomogeneous peak intensities with less number of peaks comparing than the number of amino acids in the construct. It indicated that optimization should be necessary for detailed further structural studies.