Results 141 to 150 of about 9,164 (166)
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Genetics of paraoxonase

Annals of Human Genetics, 1981
SUMMARYDanish family material comprising 1664 unrelated individuals (parents) and 3169 children, as well as 699 grandparents of the same families, were examined for paraoxonase activity. A micro‐autoanalyser method, comprising a primary testing in tris buffer at pH 7‐5 and, in the case of primarily intermediate individuals, a secondary testing at pH 10,
H, Eiberg, J, Mohr
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Paraoxonase polymorphism in rabbits

Chemico-Biological Interactions, 1999
Paraoxonase in serum and liver of rabbits and cattle was investigated. In serum the two substrates paraoxon and phenylacetate are exclusively hydrolyzed by alpha-lipoprotein-bound paraoxonase. In rabbit liver paraoxon is hydrolyzed only by paraoxonase, while phenylacetate is hydrolyzed by paraoxonase (20%) and additionally by an organophosphate ...
R, Zech   +3 more
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Paraoxonase activity and dementia

Journal of the Neurological Sciences, 2009
Paraoxonase activity, homocysteine level and lipids were determined in 120 patients with dementia (51 with Alzheimer disease, 28 with dementia of vascular origin, 41 with mixed dementia), 45 with mild cognitive impairment and in 61 age and sex matched controls without dementia.
Hanna, Wehr   +6 more
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Paraoxonase: A multifaceted biomolecule

Clinica Chimica Acta, 2009
Paraoxonase enzyme was first identified as a protective barrier against organophosphorus poisoning. After painstaking research spanning the last three decades, the knowledge about this enzyme has increased immensely. The present review attempts to elaborate the role of paraoxonase enzyme in normal physiology as well as provide an overview of the ...
Binita, Goswami   +3 more
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Metals and Paraoxonases

2017
The paraoxonases (PONs) are a three-gene family which includes PON1, PON2, and PON3. PON1 and PON3 are synthesized primarily in the liver and a portion is secreted in the plasma, where they are associated with high-density lipoproteins (HDLs), while PON2 is an intracellular enzyme, expressed in most tissues and organs, including the brain.
Costa, Lucio G.   +4 more
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Paraoxonases and infectious diseases

Clinical Biochemistry, 2017
The paraoxonases (PON1, PON2 and PON3) are an enzyme family with a high structural homology. All of them have lactonase activity and degrade lipid peroxides in lipoproteins and cells. As such, they play a role in protection against oxidation and inflammation.
Jordi, Camps   +4 more
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Paraoxonase Activity and Paraoxonase 1 Gene Polymorphism in Patients with Uremia

ASAIO Journal, 2003
Patients on hemodialysis (HD) show an increased risk for developing atherothrombotic events. The oxidative modification of low density lipoproteins (LDL) play an important role in the pathogenesis of atherosclerosis. In patients with uremia (chronic renal failure and HD), the increased oxidative stress induces oxidative modification of LDL.
Stefano, Biasioli   +6 more
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Paraoxonase 1 L55M, Q192R and paraoxonase 2 S311C alleles in atherothrombosis

Molecular and Cellular Biochemistry, 2012
Increased oxidative stress is known to play a role in the pathogenesis of atherosclerosis, and polymorphisms in genes encoding for enzymes involved in modulation of oxidant stress, such as paraoxonases (PONs), provide a potentially powerful approach to study the risk of disease susceptibility. Aim of our study is to investigate the possible association
Cozzi L.   +7 more
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Targeting paraoxonase-1 in atherosclerosis

Expert Opinion on Therapeutic Targets, 2013
Paraoxonase-1 (PON1) is a Ca(2+) dependent, high-density lipoprotein-associated lactonase which is capable of retarding/inhibiting low-density lipoprotein (LDL) oxidation. LDL oxidation is believed to be central to the initiation and progression of atherosclerosis, therefore, PON1 is considered to be atheroprotective.Relevant literature on PON1 was ...
Mike, Mackness, Bharti, Mackness
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Paraoxonase and coronary heart disease

Current Opinion in Lipidology, 1998
Paraoxonase (PON1) hydrolyses organophosphate insecticides and nerve gases and is responsible for determining the selective toxicity of these compounds in mammals. Human PON1 has two genetic polymorphisms giving rise to amino-acid substitutions at positions 55 and 192.
M I, Mackness   +8 more
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