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Ecto-ATPases - Recent Progress on Structure and Function (Paperback, Softcover reprint of the original 1st ed. 1997)
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Ecto-ATPases - Recent Progress on Structure and Function (Paperback, Softcover reprint of the original 1st ed. 1997)
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It has been known for almost 50 years that many cells carry enzymes
that hydro- lyze extracellular ATP, and the term "ecto-ATPase" was
used first by Engelhardt 40 years ago. But until the end of the
1970's, the idea of an ATPase with its ATP hydrolyzing site on the
outside of the cell membrane was met with substantial skepticism
since it was thought that ATP was strictly intracellular.
Nevertheless, ecto-ATPase activity was dem- onstrated using a
variety of intact cells. Most ecto-ATPase(s) exhibited three common
2 characteristics: 1) activation by either Ca + or Mg2+, 2)
insensitivity to the commonly used inhibitors ofF-type, P-type, and
V-type ATPases, and 3) ability to hydrolyze nucleo- side
triphosphates and often nucleoside diphosphates as well. At the
same time, the dominant ATPase activity in many plasma membrane
preparations was shown to be dis- tinct from the ion-pump ATPases,
but had similar enzymatic properties as the ecto-AT- Pase(s). Thus
the term "E-type ATPase activity" has been proposed for ATPase
activity exhibiting these characteristics, and it is assumed that
all ecto-ATPases are E-type AT- Pases. The converse is not true,
however, since soluble E-type ATPases were shown to ex- sist in
plants, microorganisms, and the saliva of blood sucking insects.
These enzymes could be easily purified, and exhibited very high
specific activity.
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