Routes to chaos in the peroxidase-oxidase reaction

2008 ◽  
pp. 252-272 ◽  
Author(s):  
Marcus J. B. Hauser ◽  
Lars Folke Olsen
Keyword(s):  
Routes To Chaos ◽  
Oxidase Reaction

Routes to Chaos in the Peroxidase−Oxidase Reaction:  Period-Doubling and Period-Adding

1997 ◽  
Vol 101 (25) ◽  
pp. 5075-5083 ◽  
Author(s):  
Marcus J. B. Hauser ◽  
Lars F. Olsen ◽  
Tatiana V. Bronnikova ◽  
William M. Schaffer
Keyword(s):  
Period Doubling ◽  
Routes To Chaos ◽  
Oxidase Reaction

Routes to Chaos in the Peroxidase−Oxidase Reaction. 2. The Fat Torus Scenario

1998 ◽  
Vol 102 (3) ◽  
pp. 632-640 ◽  
Author(s):  
Tatiana V. Bronnikova ◽  
William M. Schaffer ◽  
Marcus J. B. Hauser ◽  
Lars F. Olsen
Keyword(s):  
Routes To Chaos ◽  
Oxidase Reaction

Routes to chaos in continuous mechanical systems: Part 2. Modelling transitions from regular to chaotic dynamics

2012 ◽  
Vol 45 (6) ◽  
pp. 709-720 ◽  
Author(s):  
A.V. Krysko ◽  
J. Awrejcewicz ◽  
I.V. Papkova ◽  
V.A. Krysko
Keyword(s):  
Chaotic Dynamics ◽  
Mechanical Systems ◽  
Routes To Chaos

scholarly journals Role of the divalent metal cation in the pyruvate oxidase reaction.

1982 ◽  
Vol 257 (16) ◽  
pp. 9605-9611
Author(s):  
R Blake ◽  
T A O'Brien ◽  
R B Gennis ◽  
L P Hager
Keyword(s):  
Metal Cation ◽  
Divalent Metal ◽  
Pyruvate Oxidase ◽  
Divalent Metal Cation ◽  
Oxidase Reaction

scholarly journals Complexity of a Peroxidase-Oxidase Reaction Model

2021 ◽  
Author(s):  
Jason Gallas ◽  
Marcus Hauser ◽  
Lars Folke Olsen
Keyword(s):  
Chemical Reaction ◽  
Mixed Mode ◽  
Period Doubling ◽  
Reaction Model ◽  
Chaotic Behaviour ◽  
Mixed Mode Oscillations ◽  
Oscillating Reaction ◽  
Oxidase Reaction

The peroxidase-oxidase oscillating reaction was the first (bio)chemical reaction to show chaotic behaviour. The reaction is rich in bifurcation scenarios, from period-doubling to peak-adding mixed mode oscillations. Here, we study...

A Gut Oxidase Reaction

Science ◽  
2005 ◽  
Vol 310 (5749) ◽  
pp. 741.8-741
Keyword(s):  
Oxidase Reaction

Histochemical studies of dopa oxidase and peroxidase in the mantle-edge of the freshwater gastropod, Helisoma duryi eudiscus (Pilsbry)

1968 ◽  
Vol 46 (2) ◽  
pp. 165-167 ◽  
Author(s):  
S. P. Kapur ◽  
M. A. Gibson
Keyword(s):  
Positive Reaction ◽  
Protein Component ◽  
Negative Reaction ◽  
Structural Proteins ◽  
Freshwater Gastropod ◽  
Helisoma Duryi ◽  
Mantle Edge ◽  
Dopa Oxidase ◽  
Oxidase Reaction

The mantle-edge gland produces the highly tanned, densely fibrous periostracum, and the cubocolumnar cells contribute to the deposition of the less highly tanned matrix of the inner shell layers. The mantle-edge gland gives positive reactions for dopa oxidase and peroxidase, but does not contain melanin. The cubocolumnar cells reveal a positive reaction for dopa oxidase, possess numerous melanin granules, and exhibit a negative reaction for peroxidase. It is suggested that quinones may contribute to the process of tanning and hardening of the structural proteins of the shell. The dopa oxidase reaction within the cubocolumnar cells indicates the presence of tyrosine and suggests that these cells are capable of producing quinones to color and harden the protein component of the inner shell layers. It also explains the abundance of melanin granules within these cells. Within the mantle-edge gland, it is suggested that the peroxidase inhibits the formation of melanin from dopa quinone, and peroxidase, by accentuating quinone production, may cause further hardening of the periostracum.

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