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The phosphorylation of red blood cell membrane fragments (RBCMF) during Ca++ transport was investigated. When red cell membrane fragments are incubated with [gamma-32P]ATP under the experimental condition which minimizes the phosphorylation of Na+-K+-ATPase, RBCMF are labeled in the presence of Mg++ without Ca++. When Ca++ is added, the labeling decreases due to dephosphorylation of RBCMF. The initial reaction of phosphorylation is reversed in the presence of excess ADP. The treatment of RBCMF with n-ethylmaleimide (NEM) does not interfere with the initial phosphorylation reaction, but blocks the dephosphorylation in the presence of Ca++. These data suggest that the enzymatic sequence of the Ca++ transport mechanism may be very similar to that of the Na+ transport mechanism.
Y N Cha, and
K S Lee
December 1988,
The Biochemical journal,
Y N Cha, and
K S Lee
January 1988,
Zhonghua nei ke za zhi,
Y N Cha, and
K S Lee
January 1989,
Acta dermato-venereologica. Supplementum,
Y N Cha, and
K S Lee
May 1975,
Biochimica et biophysica acta,
Y N Cha, and
K S Lee
February 1977,
Blood,
Y N Cha, and
K S Lee
May 2008,
Current opinion in hematology,
Y N Cha, and
K S Lee
May 1978,
FEBS letters,
Y N Cha, and
K S Lee
May 1982,
Cell calcium,
Y N Cha, and
K S Lee
January 1979,
Progress in neuro-psychopharmacology,
Y N Cha, and
K S Lee
January 1967,
The Journal of clinical investigation,
