Glutathione-linked enzyme activities in red cell aging

1986 ◽  
Vol 159 (1) ◽  
pp. 73-76 ◽  
Author(s):  
Hitoshi Imanishi ◽  
Tetsuro Nakai ◽  
Tatsuo Abe ◽  
Tatsuro Takino
FEBS Letters ◽  
1980 ◽  
Vol 120 (2) ◽  
pp. 264-266 ◽  
Author(s):  
Mauro Magnani ◽  
Vilberto Stocchi ◽  
Marina Dachà ◽  
Franco Canestrari ◽  
Giorgio Fornaini
Keyword(s):  
Red Cell ◽  

Blood ◽  
1983 ◽  
Vol 61 (3) ◽  
pp. 500-506 ◽  
Author(s):  
CF Whitfield ◽  
LM Mylin ◽  
SR Goodman

Abstract Two mammalian species (porcine and murine) have erythrocytes that are being widely used to study membrane protein synthesis and red cell aging. Erythrocytes of these species however, are significantly smaller than those of the human. Before results obtained from study of these red cells can be applied to human cells, the membrane skeleton of these species must be investigated to determine if the skeletal elements are equivalent. Both pig and mouse bands 4.1b were of lower molecular weight than human 4.1b, and the a/b ratio was lower. In each species, 4.1a and b were sequence-related phosphoproteins, and yielded substantially different one-dimensional peptide maps. Band 3 of pig and mouse erythrocytes had a higher molecular weight than human band 3 and also had differing one-dimensional peptide maps after limited proteolytic cleavage with three different enzymes. In each species, free band 3 and band 3 bound to the membrane skeleton had identical peptide maps. Other major membrane skeletal components (spectrin, actin, and bands 2.1 and 4.2) seem to be very similar in molecular weight in various species. These results demonstrate that the molecular weights and relative proportions of the membrane skeletal elements are species dependent.


Vox Sanguinis ◽  
1981 ◽  
Vol 40 (2) ◽  
pp. 85-90
Author(s):  
Yoji Ishida ◽  
Shiro Miwa ◽  
Susumu Takegawa ◽  
Noboru Fujinami ◽  
Kunio Yamato

Sign in / Sign up

Export Citation Format

Share Document