ASSAY OF ORNITHINE AMINOTRANSFERASE WITH NINHYDRIN

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We developed an assay system for ornithine amino-transferase (EC 2.6.1.13) using ninhydrin. Pyrroline 5-carboxylate, a product of enzymatic transamination, reacts with ninhydrin under hot acidic conditions to form a reddish pigment soluble in ethanol. The millimolar extinction coefficient of reaction product dissolved in ethanol was 16.5 at 510 nm. Acidification with perchloric acid effectively abolished the interfering color development by L-ornithine and L-glutamate. The paired activity measurement in mouse tissues by ninhydrin and o-aminobenzaldehyde methods showed a good correlation (gamma = 0.985). In our ninhydrin method, stable ninhydrin replaced unstable o-aminobenzaldehyde, and sensitivity was much higher than that with the conventional o-aminobenzaldehyde method. (C) 1994 Academic Press, Inc.
Publisher
ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS
Issue Date
1994-12
Language
English
Article Type
Article
Citation

ANALYTICAL BIOCHEMISTRY, v.223, no.2, pp.205 - 207

ISSN
0003-2697
DOI
10.1006/abio.1994.1574
URI
http://hdl.handle.net/10203/318633
Appears in Collection
MSE-Journal Papers(저널논문)
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