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. Author manuscript; available in PMC: 2008 Dec 8.
Published in final edited form as: Biochemistry. 2005 May 31;44(21):7830–7843. doi: 10.1021/bi0500877

Table 3.

Comparison of Ca2+-Dependent TGase Activity with KGDHC, GDH, and mitAspAT Activities in Mitoplasts (P7) Derived from Nonsynaptosomal Mouse Brain Mitochondriaa

enzyme specific
activityb
recovery in P7
relative to homogenate (H) %
KGDHC 108, 129 4.0, 8.8
GDH 97, 52 3.5, 4.9
mitAspAT 657, 453 5.0, 4.3
TGase 4.3 ± 1.5c (6.4, 1.5, 5.0) 0.14 ± 0.04
a

The data were obtained from two of the mouse brain preparations described in Table 2. In the case of TGase, activity was measured in an additional preparation so that the values shown for this enzyme are for n = 3. The actual values are shown in parentheses. The protein concentrations in the nonsynaptosomal mitochondrial fraction (P6; Table 2) and the mitoplast fraction (P7) were 48 and 58.4, and 20 and 37.8 mg/mL, respectively.

b

Units are nmol min−1 (mg of protein)−1, except TGase, where specific activity is expressed as pmol h−1 (mg of protein)−1.

c

Different from zero with p < 0.05 by the one-tailed t test; p < 0.001 by the χ2 test; 95% confidence interval from −2.0 to 10.6.