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Transaminating Processes Involving Histidine in Human Haemolysed Erythrocytes

B. Štraus ; Institute of Biochemistry, Faculty of Pharmacy, University of Belgrade, Belgrade, Serbia, Yugoslavia
I. Berkeš ; Institute of Biochemistry, Faculty of Pharmacy, University of Belgrade, Belgrade, Serbia, Yugoslavia

Sažetak

Haemolysates of human red blood c ells show transaminating
activity not only between a-ketoglutaric acid and both alanine and
aspartic acid, but with other amino acids not observed previousl y.
The behaviour of h istidine in particular was studied in these
reactions since, by incubation with a-ketoglutaric acid, glutamic
acid was formed, but with pyruvate aspartic acid was unexpectedly
found.
The presence of aspartic acid was demonstrated by paper
chromatography in different solvents and by paper electrophoresis.
Imidazole derivatives were detected with Pauly's reagent.
A reaction scheme is proposed whereby pyruvate enters partly
a transaminating process with histidine, from which the resulting
imidazolyl-pyruvate gives imidazolyl-acetate by decarboxylation.
The carbon dioxide released in this process reacts with pyruvate
in a Wood-Werkmann reaction, giving rise to oxaloacetate, from
which aspartic acid is finally formed by a secondary amino-transfering
reaction with surplus histidine.
Imidazole acetate was detected by paper chromatography, and
imidazole pyruvate by the enol-borate tautomerase m ethod.

Ključne riječi

Hrčak ID:

208171

URI

https://hrcak.srce.hr/208171

Datum izdavanja:

25.8.1966.

Posjeta: 678 *