scholarly journals Bioseparation of Four Proteins fromEuphorbia characiasLatex: Amine Oxidase, Peroxidase, Nucleotide Pyrophosphatase/Phosphodiesterase, and Purple Acid Phosphatase

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.

Author(s):  
Hannah Russell ◽  
Rachel Stewart ◽  
Christopher Prior ◽  
Vasily S. Oganesyan ◽  
Thembaninkosi G. Gaule ◽  
...  

AbstractIn the study of biological structures, pulse dipolar spectroscopy (PDS) is used to elucidate spin–spin distances at nanometre-scale by measuring dipole–dipole interactions between paramagnetic centres. The PDS methods of Double Electron Electron Resonance (DEER) and Relaxation Induced Dipolar Modulation Enhancement (RIDME) are employed, and their results compared, for the measurement of the dipolar coupling between nitroxide spin labels and copper-II (Cu(II)) paramagnetic centres within the copper amine oxidase from Arthrobacter globiformis (AGAO). The distance distribution results obtained indicate that two distinct distances can be measured, with the longer of these at c.a. 5 nm. Conditions for optimising the RIDME experiment such that it may outperform DEER for these long distances are discussed. Modelling methods are used to show that the distances obtained after data analysis are consistent with the structure of AGAO.


2011 ◽  
Vol 67 (a1) ◽  
pp. C225-C225
Author(s):  
H. Yamaguchi ◽  
M. Kataoka ◽  
H. Oya ◽  
A. Tominaga ◽  
M. Ohtsu ◽  
...  

2012 ◽  
Vol 22 (18) ◽  
pp. 5784-5790 ◽  
Author(s):  
Jieyin Sun ◽  
Hiroyuki Morita ◽  
Guoshen Chen ◽  
Hiroshi Noguchi ◽  
Ikuro Abe

1997 ◽  
Vol 119 (40) ◽  
pp. 9424-9437 ◽  
Author(s):  
Elisabeth Lambert ◽  
Barbara Chabut ◽  
Sylvie Chardon-Noblat ◽  
Alain Deronzier ◽  
Geneviève Chottard ◽  
...  

2018 ◽  
Vol 9 ◽  
Author(s):  
Youbin Kong ◽  
Xihuan Li ◽  
Bing Wang ◽  
Wenlong Li ◽  
Hui Du ◽  
...  

2012 ◽  
Vol 80 (5) ◽  
pp. 665-674 ◽  
Author(s):  
Daniel Feder ◽  
Waleed M. Hussein ◽  
Daniel J. Clayton ◽  
Meng-Wei Kan ◽  
Gerhard Schenk ◽  
...  

1999 ◽  
Vol 260 (3) ◽  
pp. 709-716 ◽  
Author(s):  
Atila Durmus ◽  
Christoph Eicken ◽  
Bernd Horst Sift ◽  
Andreas Kratel ◽  
Reinhard Kappl ◽  
...  

RSC Advances ◽  
2020 ◽  
Vol 10 (63) ◽  
pp. 38631-38639
Author(s):  
Mitsuo Shoji ◽  
Takeshi Murakawa ◽  
Mauro Boero ◽  
Yasuteru Shigeta ◽  
Hideyuki Hayashi ◽  
...  

Copper amine oxidases catalyze the oxidative deamination of biogenic amines. We investigated the unique protonation states in the active site using first-principle calculations.


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