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A cadmium-binding protein of Mr about 40,000 (40K Cd-BPa) was detected in rat liver by Western blotting [Aoki, Kunimoto, Shibata & Suzuki (1986) Anal. Biochem. 157, 117-122]. It was characterized and identified as ornithine carbamoyltransferase (OCTase, EC 2.1.3.3) on the basis of coincidence of their physicochemical and enzymological features. The amino acid sequence of the N-terminal and those of three tryptic digests in 40K Cd-BPa were identical with those of OCTase. The Mr values of the denatured and native forms of 40K Cd-BPa (39,000 and 110,000 respectively) were the same as those of OCTase. 40K Cd-BPa showed, as OCTase activity, a specific activity of 230 mumol/min per mg of protein and Km of 0.6 mM for ornithine, this value also being essentially the same as that for OCTase. A rabbit antibody against OCTase reacted with 40K Cd-BPa. The native form of 40K Cd-BPa bound to 0.8 molar equiv, of cadmium, with a dissociation constant of 7.6 x 10(-6) M.
Y Aoki, and
H Sunaga, and
K T Suzuki
March 1989,
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Y Aoki, and
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K T Suzuki
January 1969,
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Y Aoki, and
H Sunaga, and
K T Suzuki
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Y Aoki, and
H Sunaga, and
K T Suzuki
January 2014,
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Y Aoki, and
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January 1975,
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Y Aoki, and
H Sunaga, and
K T Suzuki
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Y Aoki, and
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K T Suzuki
March 1968,
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society,
Y Aoki, and
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K T Suzuki
March 1982,
European journal of biochemistry,
Y Aoki, and
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K T Suzuki
November 1977,
Nature,
Y Aoki, and
H Sunaga, and
K T Suzuki
October 1983,
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