B. Ortwerth

Publications142
h-index35
Citations3,535
Highly Influential Citations66
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The non-oxidative degradation of ascorbic acid at physiological conditions.
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Regulation of tissue oxygen levels in the mammalian lens
TLDR
The distribution of mitochondria was mapped in living lenses by 2‐photon microscopy and it was found that a steep gradient of PO2 was maintained within the tissue, leading to PO2 < 2 mmHg in the core, indicating the presence of non‐mitochondrial oxygen consumers.
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Quantitation of the Singlet Oxygen Produced by UVA Irradiation of Human Lens Proteins
TLDR
The average value (2.2 mM of 1O2) corresponds to the theoretical production of 30 nmol of singlet oxygen at UVA light intensities equivalent to a 1 h exposure to sunlight at noon in the northern hemisphere.
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Vitamin C mediates chemical aging of lens crystallins by the Maillard reaction in a humanized mouse model
TLDR
Data strongly implicate vitamin C in lens crystallin aging and may serve as a model for protein aging in other tissues particularly rich in vitamin C, such as the hippocampal neurons and the adrenal gland.
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Activation of protein-bound copper ions during early glycation: study on two proteins.
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High correlation between pentosidine protein crosslinks and pigmentation implicates ascorbate oxidation in human lens senescence and cataractogenesis.
TLDR
The results suggest that redox imbalance in cellular senescent systems such as the ocular lens may lead to irreversible ascorbate oxidation and protein crosslinking by xylosone, which may play an important role in the pathogenesis of "brunescent" cataracts.
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Glycation by ascorbic acid oxidation products leads to the aggregation of lens proteins.
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The generation of superoxide anions in glycation reactions with sugars, osones, and 3-deoxyosones.
TLDR
Amadori compounds composed of lysine and short chain sugars can rapidly generate superoxide anion in the absence of metal ions.
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Correlation between a specific isoaccepting lysyl transfer ribonucleic acid and cell division in mammalian tissues.
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Bovine lens acylpeptide hydrolase. Purification and characterization of a tetrameric enzyme resistant to urea denaturation and proteolytic inactivation.
TLDR
The data show that the split enzyme is as active as the native enzyme towards the synthetic substrate Ac-Ala-p-nitroanilide, and the enzyme activity decreases with increasing urea, but 15% of the activity remains even in the presence of 6.0 M urea.
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