| MadSci Network: Biochemistry |
I suggest you hit up your library for the following journal article. It should at least give you a starting point:
Guo, MK and Messer HH (1978) A comparison of Ca2+-, Mg2+-ATPase and alkaline phosphatase activities of rat incisor pulp. Calcified Tissue International 26(1), 33-38. (Calcified Tissue International is also known as Calcified Tissue Research).
Here is the abstract:
A plasma membrane preparation derived from incisor pulps of 250-g rats was
used as the source of alkaline phosphatase and an ATPase activated by
either Ca2+ or Mg2+. Properties of the two enzymes were then compared under
a variety of experimental conditions to determine if ATPase activity is
clearly distinct from alkaline phosphatase activity. (a) The optimum pH for
ATP hydrolysis was 8.0, compared with 10.2 forp-nitrophenylphosphate. (b)
At the optimum pH, ATP hydrolysis required either Ca2+ or Mg2+ for
activation, whereasp-nitrophenylphosphate hydrolysis did not require and
was little influenced by the presence of divalent cations. (c) Alkaline
phosphatase showed maximal activity at 40°C and ATPase at 50°C, with
complete inactivation at 60°C and 70°C, respectively. (d) When the plasma
membrane preparation was preincubated in the absence of substrate at
varying temperatures of pH, alkaline phosphatase was less stable than
ATPase at extreme pH and high temperatures. (e) Alkaline phosphatase
activity was lost more rapidly than ATPase activity during storage at 4°C
for up to 10 days. (f) Butanol extraction of the plasma membrane
preparation to remove phospholipid destroyed ATPase activity and enhanced
alkaline phosphatase activity approximately fivefold. On the basis of these
comparisons it is concluded that ATP hydrolysis andp-nitrophenyl-phosphate
hydrolysis are the result of separate enzyme activities.
Try the links in the MadSci Library for more information on Biochemistry.