Effect of hydrogen peroxide on amino acid concentrations in bovine retina and vitreous humor, ex vivo

Author(s):  
A.M. LeDay ◽  
S. Ganguly ◽  
K.H. Kulkarni ◽  
A. Dash ◽  
C.A. Opere ◽  
...  
2009 ◽  
Vol 9 (1) ◽  
Author(s):  
Joshua S Davis ◽  
Christabelle J Darcy ◽  
Kim Piera ◽  
Yvette R McNeil ◽  
Tonia Woodberry ◽  
...  

2008 ◽  
Vol 53 (3) ◽  
pp. 730-733 ◽  
Author(s):  
Eloy Girela ◽  
Enrique Villanueva ◽  
Pilar Irigoyen ◽  
Victorino Girela ◽  
Claudio Hernández-Cueto ◽  
...  

1982 ◽  
Vol 48 (03) ◽  
pp. 277-282 ◽  
Author(s):  
I Nathan ◽  
A Dvilansky ◽  
T Yirmiyahu ◽  
M Aharon ◽  
A Livne

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.


1991 ◽  
Vol 56 (4) ◽  
pp. 923-932
Author(s):  
Jana Stejskalová ◽  
Pavel Stopka ◽  
Zdeněk Pavlíček

The ESR spectra of peroxidase systems of methaemoglobin-ascorbic acid-hydrogen peroxide and methaemoglobin-haptoglobin complex-ascorbic acid-hydrogen peroxide have been measured in the acetate buffer of pH 4.5. For the system with methaemoglobin an asymmetrical signal with g ~ 2 has been observed which is interpreted as the perpendicular region of anisotropic spectrum of superoxide radical. On the other hand, for the system with methaemoglobin-haptoglobin complex the observed signal with g ~ 2 is symmetrical and is interpreted as a signal of delocalized electron. After realization of three repeatedly induced peroxidase processes the ESR signal of the perpendicular part of anisotropic spectrum of superoxide radical is distinctly diminished, whereas the signal of delocalized electron remains practically unchanged. An amino acid analysis of methaemoglobin along with results of the ESR measurements make it possible to derive a hypothesis about the role of haptoglobin in increasing of the peroxidase activity of methaemoglobin.


1982 ◽  
Vol 4 (1) ◽  
pp. 73-78 ◽  
Author(s):  
Ryan J. Huxtable ◽  
Hugh Laird ◽  
Douglas Bonhaus ◽  
A. Cole Thies

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