Absence of one component of spectrin adenosine triphosphatase in hereditary spherocytosis.

نویسندگان

  • F H Kirkpatrick
  • G M Woods
  • P L La Celle
چکیده

The stimulation by calcium and magnesium of ATPase activity of isolated ghosts, of water-soluble protein (spectrin), and of residual vesicles, derived from normal erythrocytes and from hereditary spherocytes (H.S.), has been measured. The ATPase activity found in normal water-soluble protein (WSP) at low levels of calcium (0.1-2.0 mM) is essentially absent in H.S. water-soluble protein, but the ATPase activity with magnesium and with high levels of calcium (60-100 mM) is the same in H.S. and normal WSP. Compared to normal, H.S. ghosts have increased Mg2+-stimulated activity. This increased activity is retained by the sedimentable vesicles ("residue") after extraction of the ghosts with 0.025 mM EDTA. The Ca2+, Mg2+-ATPase associated with the calcium pump is not significantly different in H.S.

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عنوان ژورنال:
  • Blood

دوره 46 6  شماره 

صفحات  -

تاریخ انتشار 1975