scholarly journals Fabrication and structural characterization of Fe‑Al‑based laminated composites

Author(s):  
F. I. Rudnitski ◽  
I. V. Rafalski ◽  
P. E. Lushchik ◽  
A. I. Pokrovski ◽  
V. V. Petrenko

The paper presents the results of experimental studies of the structural characteristics of layered composites based on the Fe‑Al system; obtained using various solid‑phase methods of material deformation (hydropercussion stamping; cross‑wedge rolling) and a liquid‑phase (metallurgical) method for producing multilayer composites.

RSC Advances ◽  
2015 ◽  
Vol 5 (50) ◽  
pp. 39889-39898 ◽  
Author(s):  
Fanny Nascimento Costa ◽  
Tiago F. da Silva ◽  
Eduardo Miguez B. Silva ◽  
Regina C. R. Barroso ◽  
Delson Braz ◽  
...  

Synthesis and structural characterization of LASSBIO 1601: a cyclohexyl-N-acylhydrazone derivative.


2007 ◽  
Vol 2007 (10) ◽  
pp. 1653-1658 ◽  
Author(s):  
Donocadh P. Lydon ◽  
Peiyi Li ◽  
Andrew C. Benniston ◽  
William McFarlane ◽  
Ross W. Harrington ◽  
...  

2013 ◽  
Vol 1043 ◽  
pp. 109-115 ◽  
Author(s):  
Aleksandra Drzewiecka ◽  
Anna E. Koziol ◽  
Marta Struga ◽  
Tomas Pena Ruiz ◽  
Manuel Fernandez Gomez ◽  
...  

1986 ◽  
Vol 56 (03) ◽  
pp. 271-276 ◽  
Author(s):  
Marie-Pascale Croissant ◽  
Hendrik vande Pol ◽  
Helen H Lee ◽  
Jean-Pierre Allain

SummaryFour monoclonal anti-VIII: C antibodies were obtained from the fusion of the splenocytes of one B alb/C mouse with a specific activity ranging from 2.3 to 45,000 U/mg when purified from ascitic fluid. Only one antibody was able to inhibit completely Factor VIII: C in normal plasma. The four antibodies could bind Factor VIII: CAg in plasma and commercial concentrate both in liquid and solid phase, and were suitable for immunopurification of Factor VIII :C.Three antibodies competed with polyclonal anti-VIII: CAg Fab′ in a liquid phase IRMA, and all of them were able to displace their own binding to Factor VIII: CAg. Competition studies between monoclonal antibodies for the binding to Factor VIII: CAg were performed and showed the recognition of different epitopes and various functional impact. These studies indicate that at least one antibody, with the lowest anti-VIII:C titer clearly recognizes a different epitope of VIII: C than those recognized by the others. Affinity constants ranged from 109 to 1010 l/mole.


2005 ◽  
Vol 479 (1-2) ◽  
pp. 103-106
Author(s):  
E. Rosendo ◽  
T. Díaz ◽  
J. Martínez ◽  
H. Juárez ◽  
G. Juárez

Author(s):  
Adam Shahine ◽  
Anggia Prasetyoputri ◽  
Jamie Rossjohn ◽  
Travis Beddoe

Aldo-keto reductases (AKR) are a large superfamily of NADPH-dependent oxidoreductases and play a role in detoxification of toxic metabolites. Rv2971, an AKR inMycobacterium tuberculosis, has recently been identified as a target of isoniazid, a key first-line drug against tuberculosis. Here, the cloning, expression, purification, crystallization and structural characterization of Rv2971 are described. To gain insight into its function, the crystal structure of Rv2971 was successfully determined to 1.60 Å resolution in its unliganded form. The structure exhibits a TIM-barrel fold typical of AKRs, revealing structural characteristics essential for function and substrate specificities, allowing a structural comparison between Rv2971 and other mycobacterial AKRs.


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