The inhibition of ATP-dependent shape change of human erythrocyte ghosts correlates with an inhibition of Mg2+-ATPase activity by fluoride and aluminofluoride complexes

1992 ◽  
Vol 48 (4) ◽  
pp. 356-366 ◽  
Author(s):  
Michael B. Morris ◽  
Gregory Monteith ◽  
Basil D. Roufogalis
Keyword(s):  
Atpase Activity ◽  
Human Erythrocyte ◽  
Shape Change ◽  
Erythrocyte Ghosts

Ca2+- and Mg-ATP-dependent shape change of human erythrocyte ghosts and Triton shells

1984 ◽  
Vol 151 (1) ◽  
pp. 160-170 ◽  
Author(s):  
Yoshinori Jinbu ◽  
Shingo Sato ◽  
Makoto Nakao ◽  
Sachiko Tsukita
Keyword(s):  
Human Erythrocyte ◽  
Shape Change ◽  
Erythrocyte Ghosts

Role of spectrin in membrane fusion and in shape change of human erythrocyte ghost

1978 ◽  
Vol 36 (2) ◽  
pp. 328-329
Author(s):  
Hideo Hayashi ◽  
Yoshikazu Hirai ◽  
John T. Penniston
Keyword(s):  
Conformational Changes ◽  
Human Erythrocyte ◽  
Shape Change ◽  
Membrane Surface ◽  
Slight Modification ◽  
Active Role ◽  
Main Role ◽  
Bank Blood ◽  
Human Erythrocyte Ghost

Spectrin is a membrane associated protein most of which properties have been tentatively elucidated. A main role of the protein has been assumed to give a supporting structure to inside of the membrane. As reported previously, however, the isolated spectrin molecule underwent self assemble to form such as fibrous, meshwork, dispersed or aggregated arrangements depending upon the buffer suspended and was suggested to play an active role in the membrane conformational changes. In this study, the role of spectrin and actin was examined in terms of the molecular arrangements on the erythrocyte membrane surface with correlation to the functional states of the ghosts.Human erythrocyte ghosts were prepared from either freshly drawn or stocked bank blood by the method of Dodge et al with a slight modification as described before. Anti-spectrin antibody was raised against rabbit by injection of purified spectrin and partially purified.

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