Amine oxidase from Euphorbia characias : Kinetic and structural characterization

2017 ◽  
Vol 65 (1) ◽  
pp. 81-88 ◽  
Author(s):  
Francesca Pintus ◽  
Annalaura Sabatucci ◽  
Mauro Maccarrone ◽  
Enrico Dainese ◽  
Rosaria Medda
2013 ◽  
Vol 32 (6) ◽  
pp. 435-441 ◽  
Author(s):  
Francesca Pintus ◽  
Delia Spanò ◽  
Giovanni Floris ◽  
Rosaria Medda

2011 ◽  
Vol 2011 ◽  
pp. 1-7 ◽  
Author(s):  
Rosaria Medda ◽  
Francesca Pintus ◽  
Delia Spanò ◽  
Giovanni Floris

This paper deals with the purification of four proteins fromEuphorbia characiaslatex, a copper amine oxidase, a nucleotide pyrophosphatase/phosphodiesterase, a peroxidase, and a purple acid phosphatase. These proteins, very different in molecular weight, in primary structure, and in the catalyzed reaction, are purified using identical preliminary steps of purification and by chromatographic methods. In particular, the DEAE-cellulose chromatography is used as a useful purification step for all the four enzymes. The purification methods here reported allow to obtain a high purification of all the four proteins with a good yield. This paper will give some thorough suggestions for researchers busy in separation of macromolecules from different sources.


2007 ◽  
Vol 125 (2-3) ◽  
pp. 254-259 ◽  
Author(s):  
Mojtaba Amani ◽  
Ali A. Moosavi-Movahedi ◽  
Giovanni Floris ◽  
Anna Mura ◽  
Boris I. Kurganov ◽  
...  

2008 ◽  
Vol 475 (1) ◽  
pp. 18-24 ◽  
Author(s):  
Anna Mura ◽  
Francesca Pintus ◽  
Antonella Fais ◽  
Simona Porcu ◽  
Marcella Corda ◽  
...  

1998 ◽  
Vol 117 (4) ◽  
pp. 1363-1371 ◽  
Author(s):  
Alessandra Padiglia ◽  
Rosaria Medda ◽  
Anita Lorrai ◽  
Barbara Murgia ◽  
Jens Z. Pedersen ◽  
...  

Author(s):  
W. Allen Shannon ◽  
Hannah L. Wasserkrug ◽  
andArnold M. Seligman

The synthesis of a new substrate, p-N,N-dimethylamino-β-phenethylamine (DAPA)3 (Fig. 1) (1,2), and the testing of it as a possible substrate for tissue amine oxidase activity have resulted in the ultracytochemical localization of enzyme oxidase activity referred to as DAPA oxidase (DAPAO). DAPA was designed with the goal of providing an amine that would yield on oxidation a stronger reducing aldehyde than does tryptamine in the histochemical demonstration of monoamine oxidase (MAO) with tetrazolium salts.Ultracytochemical preparations of guinea pig heart, liver and kidney and rat heart and liver were studied. Guinea pig kidney, known to exhibit high levels of MAO, appeared the most reactive of the tissues studied. DAPAO reaction product appears primarily in mitochondrial outer compartments and cristae (Figs. 2-4). Reaction product is also localized in endoplasmic reticulum, cytoplasmic vacuoles and nuclear envelopes (Figs. 2 and 3) and in the sarcoplasmic reticulum of heart.


Author(s):  
E. Naranjo

Equilibrium vesicles, those which are the stable form of aggregation and form spontaneously on mixing surfactant with water, have never been demonstrated in single component bilayers and only rarely in lipid or surfactant mixtures. Designing a simple and general method for producing spontaneous and stable vesicles depends on a better understanding of the thermodynamics of aggregation, the interplay of intermolecular forces in surfactants, and an efficient way of doing structural characterization in dynamic systems.


Author(s):  
S. F. Hayes ◽  
M. D. Corwin ◽  
T. G. Schwan ◽  
D. W. Dorward ◽  
W. Burgdorfer

Characterization of Borrelia burgdorferi strains by means of negative staining EM has become an integral part of many studies related to the biology of the Lyme disease organism. However, relying solely upon negative staining to compare new isolates with prototype B31 or other borreliae is often unsatisfactory. To obtain more satisfactory results, we have relied upon a correlative approach encompassing a variety EM techniques, i.e., scanning for topographical features and cryotomy, negative staining and thin sectioning to provide a more complete structural characterization of B. burgdorferi.For characterization, isolates of B. burgdorferi were cultured in BSK II media from which they were removed by low speed centrifugation. The sedimented borrelia were carefully resuspended in stabilizing buffer so as to preserve their features for scanning and negative staining. Alternatively, others were prepared for conventional thin sectioning and for cryotomy using modified procedures. For thin sectioning, the fixative described by Ito, et al.


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