scholarly journals A simple, rapid and efficient isolation of erythrocyte Cu2Zn2-superoxide dismutase

1984 ◽  
Vol 221 (2) ◽  
pp. 549-551 ◽  
Author(s):  
A Gärtner ◽  
H J Hartmann ◽  
U Weser

On the basis of the thermal stability of erythrocuprein (Cu2Zn2-superoxide dismutase) a rapid preparation technique was devised and successfully employed to isolate this protein. Partial heat-deterioration of the haemolysate and subsequent chromatography of the supernatant on DEAE-Sephacel and Sephadex G-75 yielded an electrophoretically homogeneous protein within a few days. The physicochemical properties and biochemical function were identical with those reported for Cu2Zn2-superoxide dismutases prepared by established methods.

2008 ◽  
Vol 389 (9) ◽  
Author(s):  
Hester G. O'Neill ◽  
Pierre Redelinghuys ◽  
Sylva L.U. Schwager ◽  
Edward D. Sturrock

Abstract The N and C domains of somatic angiotensin-converting enzyme (sACE) differ in terms of their substrate specificity, inhibitor profiling, chloride dependency and thermal stability. The C domain is thermally less stable than sACE or the N domain. Since both domains are heavily glycosylated, the effect of glycosylation on their thermal stability was investigated by assessing their catalytic and physicochemical properties. Testis ACE (tACE) expressed in mammalian cells, mammalian cells in the presence of a glucosidase inhibitor and insect cells yielded proteins with altered catalytic and physicochemical properties, indicating that the more complex glycans confer greater thermal stabilization. Furthermore, a decrease in tACE and N-domain N-glycans using site-directed mutagenesis decreased their thermal stability, suggesting that certain N-glycans have an important effect on the protein's thermodynamic properties. Evaluation of the thermal stability of sACE domain swopover and domain duplication mutants, together with sACE expressed in insect cells, showed that the C domain contained in sACE is less dependent on glycosylation for thermal stabilization than a single C domain, indicating that stabilizing interactions between the two domains contribute to the thermal stability of sACE and are decreased in a C-domain-duplicating mutant.


2020 ◽  
Vol 11 (12) ◽  
pp. 6541-6553 ◽  
Author(s):  
Mohamed Fodil Cherif ◽  
Djalal Trache ◽  
Nicolas Brosse ◽  
Fouad Benaliouche ◽  
Ahmed Fouzi Tarchoun

2014 ◽  
Vol 16 (20) ◽  
pp. 9337-9343 ◽  
Author(s):  
Ki Jae Kim ◽  
Hyuk Kwon Kwon ◽  
Min-Sik Park ◽  
Taeeun Yim ◽  
Ji-Sang Yu ◽  
...  

Micropore formation around the ZrO2 nanoparticles is caused by the moisture adsorbed on the surface of nanoparticles. This significantly affects the physicochemical properties of the composite separators.


2012 ◽  
Vol 539 ◽  
pp. 109-114 ◽  
Author(s):  
G.S. Borghetti ◽  
J.P. Carini ◽  
S.B. Honorato ◽  
A.P. Ayala ◽  
J.C.F. Moreira ◽  
...  

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