text: Yo, check it out, listen up, I got some science to spit,
  About the ATPase activity, erythrocyte ghosts, legit.
  When ATP is present, it goes through activation, see,
  Biphasic style, with K0.5 at 20 microM and 400 microM, G.
  Vanadate comes in, inhibiting in a similar way,
  Biphasic inhibition, IC50 at 100 microM, okay?
  
  La3+ steps up, inhibiting around 70% of the game,
  IC50 at 25 microM, putting the erythrocytes to shame.
  But Cd2+ takes the crown, it's got full inhibition on lock,
  IC50 at 60 microM, shutting down the ATPase rock.
  
  We partially purify the activity, using Triton X-100 in the mix,
  Followed by chromatography over Sepharose CL-2B, slick.
  But Triton messes with the curves, distorting the vanadate's rhyme,
  And the ATP's activation, ain't it a crime?
  
  Now let's talk about Ca2+, it brings the inhibition to the floor,
  IC50 at 0.4 mM, stopping the activity galore.
  All these findings and previous studies intertwine,
  Suggesting multiple enzymes, that's the bottom line.
  
  But only the vanadate-sensitive activity takes the lead,
  Involved in erythrocyte shape change, that's indeed.
  So there you have it, the rap version of the facts,
  About the Mg(2+)-dependent ATPase activity and its tracks.