Isolation from Peas of Co-Factors and Inhibitors of Indolyl-3-Acetic Acid Oxidase

Nature ◽  
1962 ◽  
Vol 193 (4814) ◽  
pp. 456-457 ◽  
Author(s):  
MASAKI FURUYA ◽  
ARTHUR W. GALSTON ◽  
BRUCE B. STOWE
Keyword(s):  
Acetic Acid ◽  
Acid Oxidase

scholarly journals REGULATORY MECHANISMS OF CELLULAR RESPIRATION

1950 ◽  
Vol 34 (2) ◽  
pp. 211-224 ◽  
Author(s):  
E. S. Guzman Barron ◽  
Maria Isabel Ardao ◽  
Marion Hearon
Keyword(s):  
Acetic Acid ◽  
Pyruvic Acid ◽  
No Oxidation ◽  
Yeast Cells ◽  
Acid Formation ◽  
Cellular Respiration ◽  
Acid Oxidase ◽  
Acid Solutions ◽  
Fluoroacetic Acid ◽  
A Cell

The rate of the aerobic metabolism of pyruvic acid by bakers' yeast cells is determined mainly by the amount of undissociated acid present. As a consequence, the greatest rate of oxidation was observed at pH 2.8. Oxidation, at a slow rate, started at pH 1.08; at pH 9.4 there was no oxidation at all. The anaerobic metabolism, only a fraction of the aerobic, was observed only in acid solutions. There was none at pH values higher than 3. Pyruvic acid in the presence of oxygen was oxidized directly to acetic acid; in the absence of oxygen it was metabolized mainly by dismutation to lactic and acetic acids, and CO2. Acetic acid formation was demonstrated on oxidation of pyruvic acid at pH 1.91, and on addition of fluoroacetic acid. Succinic acid formation was shown by addition of malonic acid. These metabolic pathways in a cell so rich in carboxylase may be explained by the arrangement of enzymes within the cell, so that carboxylase is at the center, while pyruvic acid oxidase is located at the periphery. Succinic and citric acids were oxidized only in acid solutions up to pH 4. Malic and α-ketoglutaric acids were not oxidized, undoubtedly because of lack of penetration.

Isoperoxidases of (IAA oxidase) oxidase in oat coleoptiles

1973 ◽  
Vol 51 (11) ◽  
pp. 2047-2052 ◽  
Author(s):  
William R. Gordon ◽  
James H. M. Henderson
Keyword(s):  
Acetic Acid ◽  
Avena Sativa ◽  
Gel Electrophoresis ◽  
Enzyme Assay ◽  
Polyacrylamide Gel Electrophoresis ◽  
Acid Oxidase ◽  
Iaa Oxidase ◽  
Substrate Specificities ◽  
Electrophoretic Mobilities ◽  
Indole 3 Acetic Acid

Eight constitutive isoperoxidases were separated by the disc method of polyacrylamide gel electrophoresis from a lyophilized extract of 8-day-old oat (Avena sativa L., cv. Victory) coleoptiles. Both anodic and cathodic isoperoxidases were studied and differences in electrophoretic mobilities and hydrogen donor substrate specificities were revealed. In addition, by enzyme assay, cathodic and anodic isoenzymes were shown to possess differences in peroxidase and IAA (indole-3-acetic acid) oxidase activities.Treatment of coleoptiles with 0.07 mM IAA for 24 h resulted in the repression of two slow-migrating anodic isoperoxidases; however, the same treatment also resulted in the induction of two slow-migrating cathodic isoenzymes which were shown to exhibit peroxidase and IAA oxidase activities.

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