Determination of the Role of the Carboxyl-terminal Leucine-122 in FMN-binding Protein by Mutational and Structural Analysis

2007 ◽  
Vol 141 (4) ◽  
pp. 459-468 ◽  
Author(s):  
M. Kitamura ◽  
K. Terakawa ◽  
H. Inoue ◽  
T. Hayashida ◽  
K. Suto ◽  
...  
2018 ◽  
Vol 28 (55) ◽  
pp. 845-862
Author(s):  
Fabiana Barros Medeiros ◽  
Francieli Sant'ana Marcatto ◽  
Hélio Silveira ◽  
MariaTeresa De Nóbrega

Esta pesquisa tem como objetivo estudar a vulnerabilidade à erosão dos solos da zona de contato do arenito da Formação Caiuá com o basalto da Formação Serra Geral, no município de Araruna, Mesorregião Noroeste Paranaense, dando enfoque ao papel da estabilidade da estrutura atual dos solos, considerando-se as alterações produzidas pelas formas de uso e ocupação da área. A análise realizada também considerou as variações das características morfológicas dos solos em perfil e ao longo da litossequência (sistema pedológico), assim como os seus reflexos na geração de setores mais ou menos suscetíveis à erosão na vertente. Para o levantamento dos solos ao longo da vertente foram utilizados os procediments propostos pela Análise Estrutural da Cobertura Pedológica e a coleta de amostras para a determinação da granulometria e estabilidade de agregados. Os resultados indicaram a ação dos fluxos de água laterais e verticais, atuando na transformação dos horizontes dos solos ao longo da vertente e uma variação da estabilidade estrutural associada as características morfológicas dos solos e ao tipo de uso e manejo empregado. Os Argissolos apresentaram agregados pequenos e um gradiente textural entre o horizonte superficial e subsuperficial, lhe conferindo uma forte suscetibilidade a erosão. O Nitossolo não apresentou grande diferenciação no tamanho dos agregados, exceto no horizonte Bw, onde a redução no tamanho dos agregados se associaram a mudança morfológica da estrutura do solo.AbstractThis research aims to study the vulnerability to soil erosion of the contact zone of the sandstone Formation Caiuá with basalt of the Serra Geral Formation, in the municipality of Araruna, Paraná Northwest Region, giving focus to the role of the stability of the current structure of soils, considering the changes produced by the forms of use and occupation of the area. The analysis also considered variations of morphological characteristics of soils in profile and along the lithosactivity (pedological system), as well as your reflexes in the generation of sectors more or less susceptible to erosion in the shed. For the survey of the soils along the strand, the procedures proposed by the Structural Analysis of the Pedological Coverage and the collection of samples for the determination of the granulometry and stability of aggregates were used. The results indicated the action of the lateral and vertical water flows, acting on the transformation of the soil horizons along the slope and a variation of the structural stability associated with the morphological characteristics of the soils and the type of use and management used. The Argisols presented small aggregates and a textural gradient between the surface and subsurface horizon, giving it a strong susceptibility to erosion. The Nitossolo did not show great differentiation in the size of the aggregates, except in the Bw horizon, where the reduction in the size of the aggregates was associated to the morphological change of the soil structure.Keywords: structural analysis of the soil cover, stability of aggregates, susceptibility to erosion, pedological systems.


2015 ◽  
Vol 396 (9-10) ◽  
pp. 1127-1134 ◽  
Author(s):  
Phong T. Nguyen ◽  
Qi Wen Li ◽  
Neena S. Kadaba ◽  
Jeffrey Y. Lai ◽  
Janet G. Yang ◽  
...  

Abstract Despite the ubiquitous role of ATP-binding cassette (ABC) importers in nutrient uptake, only the Escherichia coli maltose and vitamin B12 ABC transporters have been structurally characterized in multiple conformations relevant to the alternating access transport mechanism. To complement our previous structure determination of the E. coli MetNI methionine importer in the inward facing conformation (Kadaba et al. (2008) Science 321, 250–253), we have explored conditions stabilizing the outward facing conformation. Using two variants, the Walker B E166Q mutation with ATP+EDTA to stabilize MetNI in the ATP-bound conformation and the N229A variant of the binding protein MetQ, shown in this work to disrupt methionine binding, a high affinity MetNIQ complex was formed with a dissociation constant measured to be 27 nm. Using wild type MetQ containing a co-purified methionine (for which the crystal structure is reported at 1.6 Å resolution), the dissociation constant for complex formation with MetNI is measured to be ∼40-fold weaker, indicating that complex formation lowers the affinity of MetQ for methionine by this amount. Preparation of a stable MetNIQ complex is an essential step towards the crystallographic analysis of the outward facing conformation, a key intermediate in the uptake of methionine by this transport system.


2014 ◽  
Vol 226 (03) ◽  
Author(s):  
S Hutter ◽  
PA Northcott ◽  
M Kool ◽  
SM Pfister ◽  
D Kawauchi ◽  
...  
Keyword(s):  

1987 ◽  
Vol 26 (01) ◽  
pp. 1-6 ◽  
Author(s):  
S. Selvaraj ◽  
M. R. Suresh ◽  
G. McLean ◽  
D. Willans ◽  
C. Turner ◽  
...  

The role of glycoconjugates in tumor cell differentiation has been well documented. We have examined the expression of the two anomers of the Thomsen-Friedenreich antigen on the surface of human, canine and murine tumor cell membranes both in vitro and in vivo. This has been accomplished through the synthesis of the disaccharide terminal residues in both a and ß configuration. Both entities were used to generate murine monoclonal antibodies which recognized the carbohydrate determinants. The determination of fine specificities of these antibodies was effected by means of cellular uptake, immunohistopathology and immunoscintigraphy. Examination of pathological specimens of human and canine tumor tissue indicated that the expressed antigen was in the β configuration. More than 89% of all human carcinomas tested expressed the antigen in the above anomeric form. The combination of synthetic antigens and monoclonal antibodies raised specifically against them provide us with invaluable tools for the study of tumor marker expression in humans and their respective animal tumor models.


1981 ◽  
Author(s):  
M Yamamoto ◽  
K Watanabe ◽  
Y Ando ◽  
H Iri ◽  
N Fujiyama ◽  
...  

It has been suggested that heparin caused potentiation of aggregation induced by ADP or epinephrine. The exact mechanism of heparin-induced platelet activation, however, remained unknown. In this paper, we have investigated the role of anti-thrombin III ( AT ) in heparin-induced platelet activation using purified AT and AT depleted plasma. When ADP or epinephrine was added to citrated PRP one minute after addition of heparin ( 1 u/ml, porcine intestinal mucosal heparin, Sigma Co. USA ), marked enhancement of platelet aggregation was observed, compared with the degree of aggregation in the absence of heparin. However, in platelet suspensions prepared in modified Tyrode’s solution, heparin exhibited no potentiating effect on platelet aggregation induced by epinephrine or ADP. Potentiation of epinephrine- or ADP-induced platelet aggregation by heparin was demonstrated when purified AT was added to platelet suspensions at a concentration of 20 μg/ml. AT depleted plasma, which was prepared by immunosorption using matrix-bound antibodies to AT, retained no AT, while determination of α1-antitrypsinα2- macroglobulin and fibrinogen in AT depleted plasma produced values which corresponded to those of the original plasma when dilution factor was taken into account. The activities of coagulation factors were also comparable to those of the original plasma. Heparin exhibited potentiating effect on ADP- or epinephrine-induced aggregation of platelets in original plasma, but no effect in AT depleted plasma. When purified AT was added back to AT depleted plasma at a concentration of 20 μg/ml, potentiation of platelet aggregation by heparin was clearly demonstrated.Our results suggest that effect of heparin on platelet aggregation is also mediated by anti-thrombin III.


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