Authors:
M. Králová Czechoslovak Academy of Sciences Institute of Experimental Botany Prague (Czechoslovakia)

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M. Kutáček Czechoslovak Academy of Sciences Institute of Experimental Botany Prague (Czechoslovakia)

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P. Stránský Czechoslovak Academy of Sciences Institute of Experimental Botany Prague (Czechoslovakia)

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Abstract  

Besides conventional methods, transminase activity can also be followed by an isotopically labelled substrate, i.e. by an amino acid with a15N labelled amino group. The application of the labelled substrate enables their study in vitro as well as in vivo. This method was applied for following the tryptophan transaminase activity in germinating maize plants. The enzym preparations used for in vitro analysis were purified on a Sephadex G 100 column. For in vivo experiments the15 N substrate was introduced by vacuum infiltration into the plants leaves. The amino acids originated by transamination are chromatographically separated and after purifying by paper electrophoresis, the atom excess15N is determined. In maize tissue originated glutamic acid (from infiltrated α-ketoglutarate substrate), which in the course of further reactions was transformed into aspartic acid and asparagine. The results found so far by studying the low activity of tryptophan-transaminase in vivo entitle us to improve our method of transaminase activity determination by using15N labelled-substrate.

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Journal of Radionalytical and Nuclear Chemistry
Language English
Size A4
Year of
Foundation
1968
Volumes
per Year
1
Issues
per Year
12
Founder Akadémiai Kiadó
Founder's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Publisher Akadémiai Kiadó
Springer Nature Switzerland AG
Publisher's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible
Publisher
Chief Executive Officer, Akadémiai Kiadó
ISSN 0236-5731 (Print)
ISSN 1588-2780 (Online)