ENZYMATIC TRANSAMIDINATION FROM CANAVANINE TO GLYCINE BY HOG KIDNEY EXTRACTS
- 1 September 1956
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 43 (5) , 675-681
- https://doi.org/10.1093/oxfordjournals.jbchem.a126670
Abstract
Aqueous extract of hog kidney shows the enzymic activity of amidine-transfer in the following reaction: canavanine + glycine[forward arrow] glycocyamine + canaline. Prior to glycocyamine determination by Sakaguchi''s reaction, glycocyamine was separated from canavanine and glycine by descending paper chro-matography with a solvent mixture of butanol-acetic acid-water (4:1:1), whereby the spot of glycocyamine is found at Rf 0.30. The enzymic activity is increased by the addition of ethylenediamine tetraacetate or by dialysis, but it is inhibited by Mn++, or by 0.001[image] p-chloromer-curic benzoate, which is completely restored by further addition of 0.01[image] reduced glutathione. The optimum pH of this enzyme is 7.4. The occurrence of a Michaelis enzyme-canavanine complex compound is discussed.Keywords
This publication has 3 references indexed in Scilit:
- BIOSYNTHESIS OF ARGININE FROM CANAVANINE AND ORNITHINE IN KIDNEYJournal of Biological Chemistry, 1956
- A NEW METHOD FOR THE COLORIMETRIC DETERMINATION OF ARGININEThe Journal of Biochemistry, 1950
- The preparation of canavanine from Canavalia obtusifoliaBiochemical Journal, 1939