Comparative studies on D-Glyceraldehyde-3-phosphate dehydrogenases : VIII. A Study of the Essential Zn Ions of the Enzyme

Keleti, Tamás and Telegdi, Marianna (1959) Comparative studies on D-Glyceraldehyde-3-phosphate dehydrogenases : VIII. A Study of the Essential Zn Ions of the Enzyme. ACTA PHYSIOLOGICA HUNGARICA, 15 (4). pp. 281-290. ISSN 0231-424X

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Abstract

The inhibitory action of 1,10-phenanthrolene on the D-glyceraldehyde-3-pbosphate and D-glyceraldehyde oxidation by D-glyceraldehyde-3-phosphate dehydrogenases isolated in crystalline form from rabbit, bovine and pig muscle, from baker’s and brewer’s yeast, as well as from crayfish muscle, has been studied. All these enzymes were inhibited in about the same measure, irrespective of the substrate used. Inhibition was slower when the reaction mixture contained phosphate instead of arsenate. When alloxan was used instead of diphos- phopyridine nucleotide, D-glyceraldehyde-3-phosphate dehydrogenase did not oxidize D-glyceraIdehyde-3-phosphate and its oxidative action on D-glyceraldehyde was also ques tionable

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