scholarly journals THE EFFECTS OF DIFFERENT STORING TEMPERATURES ON THE ACTIVITY OF SHEEP BLOOD AND PLASMA GLUTATHIONE PEROXIDASE

Author(s):  
Dušan BOŠNJAKOVIĆ ◽  
Aleksandra PETROVIĆ ◽  
Olivera VALČIĆ ◽  
Ivan JOVANOVIĆ ◽  
Svetlana MILANOVIĆ

The aim of the study was to determine the stability of the activity ofglutathione peroxidases 1 and 3 during storage at +40C and -180C. Blood sampleswere taken from eight sheep and the activity of the enzyme was determined in theplasma (GPx3) and erythrocytes (GPx1) on the first, third, fifth and seventh day insamples stored at +40C and after one and three months in samples stored at -180C.GPx3 activity decreased significantly during storage at both temperatures, whileGPx1 remained steady even after three months of storage at -180C. Obtained resultsindicate that GPx3 activity has to be determined in fresh sheep plasma samples,while the activity of sheep erythrocyte GPx1 can be determined even after 3 monthsof storage at -180C.

2006 ◽  
Vol 326 (1) ◽  
pp. 139-147 ◽  
Author(s):  
Tadashi Yamasaki ◽  
Koji Tahara ◽  
Shoichi Takano ◽  
Miho Inoue-Murayama ◽  
Michael T. Rose ◽  
...  

Blood ◽  
1989 ◽  
Vol 73 (1) ◽  
pp. 318-323 ◽  
Author(s):  
N Avissar ◽  
JC Whitin ◽  
PZ Allen ◽  
IS Palmer ◽  
HJ Cohen

Abstract Plasma glutathione peroxidase (GSHPx) (glutathione: H2O2 oxidoreductase) is a unique selenoglycoprotein. Treatment of this enzyme with glycopeptidase F partially deglycosylates it and establishes the presence of N-linked sugar moieties. Antibodies raised in a rabbit against the purified enzyme from plasma were found to be specific, noninhibitory, and capable of precipitating the enzymatic activity. The antibodies precipitated greater than 90% of the GSHPx activity of normal plasma, thus indicating that the selenoenzyme is the main if not the sole GSHPx activity of plasma. The antibodies did not precipitate RBC GSHPx. A slight cross-reactivity of the antibodies was found with rat plasma GSHPx. A GSHPx activity precipitation assay of normal plasma in the presence of selenium (Se)-deficient plasma indicates that no cross-reactive protein in the Se-deficient plasma interferes with the precipitation of the GSHPx activity from normal plasma. Thus, GSHPx protein as well as activity is deficient in plasma in the absence of Se. Antibodies against GSHPx either from RBCs or from plasma were used to specifically immunoprecipitate most of the GSHPx activity from RBCs or plasma, respectively, in healthy individuals to determine the amount of Se associated with the protein. GSHPx accounts for approximately 15% of the Se in RBCs and 12% of the Se in plasma. Thus, in normal individuals, these proteins account for only a fraction of plasma and RBC Se.


1988 ◽  
Vol 75 (s19) ◽  
pp. 43P-43P
Author(s):  
R.M. Berry ◽  
N.A. Punchard ◽  
N.A. MacLachlan ◽  
R.P.H. Thompson

2009 ◽  
Vol 327 (1-2) ◽  
pp. 111-126 ◽  
Author(s):  
Filomena G. Ottaviano ◽  
Shiow-Shih Tang ◽  
Diane E. Handy ◽  
Joseph Loscalzo

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