Destruction of Hydroxycinnamic Acids coupled to Oxidation of Indolyl-3-acetic Acid by Peroxidase as a Possible Mechanism for Adaptive Changes of Indolyl-3-acetic Acid Oxidase Activity

Nature ◽  
1964 ◽  
Vol 202 (4927) ◽  
pp. 88-89 ◽  
Author(s):  
G. ENGELSMA
Keyword(s):  
Acetic Acid ◽  
Oxidase Activity ◽  
Hydroxycinnamic Acids ◽  
Acid Oxidase ◽  
Adaptive Changes

Constitutive isoflavones as modulators of indole-3-acetic acid oxidase activity of acidic cell wall isoperoxidases from lupin hypocotyls

1992 ◽  
Vol 31 (11) ◽  
pp. 3681-3684 ◽  
Author(s):  
María A. Ferrer ◽  
María A. Pedreño ◽  
Romualdo Muñoz ◽  
A.Ros Barceló
Keyword(s):  
Cell Wall ◽  
Acetic Acid ◽  
Oxidase Activity ◽  
Acid Oxidase ◽  
Indole 3 Acetic Acid

Impairment of Platelet Aggregation by Echis colorata Venom Mediated by L-Amino Acid Oxidase or H2O2

1982 ◽  
Vol 48 (03) ◽  
pp. 277-282 ◽  
Author(s):  
I Nathan ◽  
A Dvilansky ◽  
T Yirmiyahu ◽  
M Aharon ◽  
A Livne
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Platelet Aggregation ◽  
Snake Venom ◽  
Oxidase Activity ◽  
Enzyme Preparation ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Hemostatic Disorders

SummaryEchis colorata bites cause impairment of platelet aggregation and hemostatic disorders. The mechanism by which the snake venom inhibits platelet aggregation was studied. Upon fractionation, aggregation impairment activity and L-amino acid oxidase activity were similarly separated from the crude venom, unlike other venom enzymes. Preparations of L-amino acid oxidase from E.colorata and from Crotalus adamanteus replaced effectively the crude E.colorata venom in impairment of platelet aggregation. Furthermore, different treatments known to inhibit L-amino acid oxidase reduced in parallel the oxidase activity and the impairment potency of both the venom and the enzyme preparation. H2O2 mimicked characteristically the impairment effects of L-amino acid oxidase and the venom. Catalase completely abolished the impairment effects of the enzyme and the venom. It is concluded that hydrogen peroxide formed by the venom L-amino acid oxidase plays a role in affecting platelet aggregation and thus could contribute to the extended bleeding typical to persons bitten by E.colorata.

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.

The Effect of Castration and Testosterone Propionate on d-Amino Acid Oxidase Activity in the Mouse

Science ◽  
1943 ◽  
Vol 98 (2534) ◽  
pp. 89-89
Author(s):  
L. C. Clark ◽  
C. D. Kochakian ◽  
R. Phyllis Fox
Keyword(s):  
Amino Acid ◽  
Oxidase Activity ◽  
Testosterone Propionate ◽  
Acid Oxidase ◽  
Amino Acid Oxidase
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