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. Author manuscript; available in PMC: 2011 Jun 1.
Published in final edited form as: Amino Acids. 2010 Mar 22;41(1):7–27. doi: 10.1007/s00726-010-0552-0

Table 3.

Relative specific activities of mAAT and cysteine S-conjugate β-lyase in fractions obtained from rat kidney mitochondria

Fraction mAAT
(mU/mg)a (A)
Cysteine S-conjugate β-
lyase (mU/mg)b (B)
A/B
Mitochondria (unfractionated)c 1316 5.4 244
Mitochondria (high-Mr fraction)d 51 0.23 222
Mitochondria (low-Mr fraction)d 2190 7.8 281
a

The reaction mixture contained 6 mM α-ketoglutarate, 10 mM L-aspartate and 100 mM potassium phosphate buffer (pH 7.4); 37°C. The rate of oxaloacetate formation was measured. One unit = one μmol/min.

b

The reaction mixture contained 10 mM TFEC, 0.1 mM α-ketoglutarate, and 100 mM potassium phosphate buffer (pH 7.4); 37°C. Pyruvate formation was determined.

c

Kidney mitochondria were prepared as described by Zhang et al. (2006) and disrupted by sonication.

d

Fractionated as noted in Table 2.